NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17539660|ref|NP_501873|]
View 

HOOK_N domain-containing protein [Caenorhabditis elegans]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-525 3.64e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 3.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAglqfennclvgKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsDSRIEMILEESK 452
Cdd:COG1196 392 LRAAAELAA-----------QLEEL----EEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAA 448
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 453 TRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
462-627 1.66e-07

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.38  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 462 IERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDR 541
Cdd:COG4942  36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 542 AGNMlITEQEIRNQTSVQYKERTSALENQLSQKDAE-IENLKRDLQQLVTKhESELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:COG4942 116 LGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEAL 193

                ....*..
gi 17539660 621 RREHEAL 627
Cdd:COG4942 194 KAERQKL 200
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-525 3.64e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 3.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAglqfennclvgKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsDSRIEMILEESK 452
Cdd:COG1196 392 LRAAAELAA-----------QLEEL----EEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAA 448
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 453 TRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
205-498 2.46e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    205 TMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKgrelkliIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKE 284
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    285 saqlLQQLEESRAALRDEQRHLEHQeaengkIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRMATN 364
Cdd:TIGR02168  304 ----KQILRERLANLERQLEELEAQ------LEELESKLDELAEELAELEEKLEEL-KEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    365 ENVDLEELLKGVTNGKAGLQFENNCLVGKLEELsfvsDRNKQDADNARAQLEEEREKHRlatEKLHQENIDYMKTSDSRI 444
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELL---KKLEEAELKELQAELEEL 445
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17539660    445 EMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQR--ALNSEMANH 498
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-629 3.80e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  213 RELKTAKKKLVDMEHMVDELESEN-RNLTEKGRELKLIIDSLKsDVTNKRDTAKSSQQREQELSNILEEKEKESAQL--- 288
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKeKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKELESLegs 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  289 -------LQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRM 361
Cdd:PRK03918 254 krkleekIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI-EKRLSRLEEEINGIEERIKE 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  362 ATNENVDLEELLK---------GVTNGKAGLQFENNCLVGKLEEL-SFVSDRNKQDADNARAQLEEEREKHRLATEKLHQ 431
Cdd:PRK03918 333 LEEKEERLEELKKklkelekrlEELEERHELYEEAKAKKEELERLkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  432 EnIDYMKTSDSRIEMILEESKTRKMM------------DESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHL 499
Cdd:PRK03918 413 R-IGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  500 QKEGIQSVETYLQmakkrIEHLELELSATNA-TIEFQSQQLDRAGNMLIT-EQEIRNQTS-----VQYKERTSALENQLS 572
Cdd:PRK03918 492 ESELIKLKELAEQ-----LKELEEKLKKYNLeELEKKAEEYEKLKEKLIKlKGEIKSLKKeleklEELKKKLAELEKKLD 566
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660  573 QKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGK 629
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
462-627 1.66e-07

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: 54.38  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 462 IERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDR 541
Cdd:COG4942  36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 542 AGNMlITEQEIRNQTSVQYKERTSALENQLSQKDAE-IENLKRDLQQLVTKhESELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:COG4942 116 LGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEAL 193

                ....*..
gi 17539660 621 RREHEAL 627
Cdd:COG4942 194 KAERQKL 200
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
219-627 4.96e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   219 KKKLVDMEHMVDELESENRNLTEKGR----ELKLIIDSlKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKlqdeNLKELIEK-KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   295 SRAALRDEqrhLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELA----SFRQKEKELIDELRMATNENVDLE 370
Cdd:pfam05483 332 EKEAQMEE---LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   371 ElLKGVTNGKAGLQFENNC-------LVGKLEELSFVSDRNKQDADNARAQL------------EEEREKHRLATEKLhq 431
Cdd:pfam05483 409 E-LKKILAEDEKLLDEKKQfekiaeeLKGKEQELIFLLQAREKEIHDLEIQLtaiktseehylkEVEDLKTELEKEKL-- 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   432 ENIDYMKTSDsrieMILEESKtrKMMDESTIERLRLdldneksyKKNLEDLLNDLNQralnsEMANHLQKEGIQSVETYL 511
Cdd:pfam05483 486 KNIELTAHCD----KLLLENK--ELTQEASDMTLEL--------KKHQEDIINCKKQ-----EERMLKQIENLEEKEMNL 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   512 qmaKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTK 591
Cdd:pfam05483 547 ---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 17539660   592 HESELKeqheQLNVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:pfam05483 624 GSAENK----QLNAYEIKVNKLELELASAKQKFEEI 655
PRK12704 PRK12704
phosphodiesterase; Provisional
550-626 1.62e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  550 QEIRNQTSVQYKERTS---ALENQLSQKDaeiENLKRDLQQLvTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEA 626
Cdd:PRK12704  67 HKLRNEFEKELRERRNelqKLEKRLLQKE---ENLDRKLELL-EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
511-623 4.82e-03

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 40.13  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   511 LQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQyKERTSALENQLSQ-------KDAEIENLKR 583
Cdd:pfam10186  28 LARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLLKSEVAIS-NERLNEIKDKLDQlrreiaeKKKKIEKLRS 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17539660   584 DLQQLVTKHES---ELKE-QHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:pfam10186 107 SLKQRRSDLESasyQLEErRASQLAKLQNSIKRIKQKWTALHSK 150
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
219-508 7.08e-03

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.


Pssm-ID: 185749 [Multi-domain]  Cd Length: 353  Bit Score: 39.65  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 219 KKKLVDmEHMVDELESENRNLTEKGRELKL--IIDSLKSDVTNKRDTAKSSQQREQE-----LSNILEEKEKESAQLLQQ 291
Cdd:cd09236  15 KDRLVN-ESIIDELEELTNRAHSTLRSLNLpgSLQALEKPLGLPPSLLRHAEEIRQEdglerIRASLDDVARLAASDRAI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQ---DASENELASFRQKEKELIDELRMATNENVD 368
Cdd:cd09236  94 LEEAMDILDDEASEDESLRRKFGTDRWTRPDSHEANPKLYTQAAEYEgylKQAGASDELVRRKLDEWEDLIQILTGDERD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 369 LEELLKGVTNGKAGLQFENNC--LVGKLEELSFVSD---------RNKQDADNARAQLEEE-----REKHRLATEKLHQE 432
Cdd:cd09236 174 LENFVPSSRRPSIPPELERHVraLRVSLEELDRLESrrrrkveraRTKARADDIRPEILREaarleREYPATEVAPAHFE 253
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 433 NI--DYMKTSDSRIEMILEESKTRkmmdESTIERLRldLDNEKSYKKNLEDLLNDLNQRALNS-EMANHLQKEGIQSVE 508
Cdd:cd09236 254 DLfdKRLAKYDKDLDAVSEEAQEQ----EEILQQIE--VANKAFLQSRKGDPATKERERALQSlDLAYFKYKEIVSNLD 326
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-525 3.64e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 3.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAglqfennclvgKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsDSRIEMILEESK 452
Cdd:COG1196 392 LRAAAELAA-----------QLEEL----EEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAA 448
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 453 TRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
205-498 2.46e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    205 TMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKgrelkliIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKE 284
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    285 saqlLQQLEESRAALRDEQRHLEHQeaengkIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRMATN 364
Cdd:TIGR02168  304 ----KQILRERLANLERQLEELEAQ------LEELESKLDELAEELAELEEKLEEL-KEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    365 ENVDLEELLKGVTNGKAGLQFENNCLVGKLEELsfvsDRNKQDADNARAQLEEEREKHRlatEKLHQENIDYMKTSDSRI 444
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELL---KKLEEAELKELQAELEEL 445
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17539660    445 EMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQR--ALNSEMANH 498
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
212-599 9.28e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 9.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    212 DRELKTAKKKLVDMEHM-------VDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKE 284
Cdd:TIGR02168  676 RREIEELEEKIEELEEKiaelekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    285 SAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEN---ELASFRQKEKELIDELRM 361
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    362 ATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSfvsdRNKQDADNARAQLEEEREKHRLATEKLhQENIDYMKTSD 441
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE----SELEALLNERASLEEALALLRSELEEL-SEELRELESKR 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    442 SRIEMILEESKTRKMMDESTIERLRLDLDneksykkNLEDLLNDLNQRalnsEMANHLQKEgiQSVETYLQMAKKRIEHL 521
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRID-------NLQERLSEEYSL----TLEEAEALE--NKIEDDEEEARRRLKRL 977
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660    522 ElelsatnatiefqsQQLDRAGNM-LITEQEIRnqtsvQYKERTSALENQlsqkDAEIENLKRDLQQLVTKHESELKEQ 599
Cdd:TIGR02168  978 E--------------NKIKELGPVnLAAIEEYE-----ELKERYDFLTAQ----KEDLTEAKETLEEAIEEIDREARER 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-622 1.46e-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: 62.00  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    272 QELSNILEE--------KEKESAQL--------LQQLEESRAALRDEQRHLEHQeAENGKIVEQLKTvsELNE-KLTMQV 334
Cdd:TIGR02168  155 EERRAIFEEaagiskykERRKETERklertrenLDRLEDILNELERQLKSLERQ-AEKAERYKELKA--ELRElELALLV 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    335 KDLQDAsENELASFRQKEKELIDELRMATNE----NVDLEELLKGVTN---GKAGLQFENNCLVGKLEELsfvsDRNKQD 407
Cdd:TIGR02168  232 LRLEEL-REELEELQEELKEAEEELEELTAElqelEEKLEELRLEVSEleeEIEELQKELYALANEISRL----EQQKQI 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    408 ADNARAQLEEEREKHRLATEKLHQENIDYmktsdsriEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLN 487
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    488 Q--RALNSEMANHLQKEGIQSVEtyLQMAKKRIEHLELELSATNATIEFQSQQLDRAG-NMLITEQEIRNQTSVQYKERT 564
Cdd:TIGR02168  379 EqlETLRSKVAQLELQIASLNNE--IERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEEL 456
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660    565 SALENQLSQKDAEIENLKRDLQQlvtkheseLKEQHEQLNVHHQSQQKLHSEAEKLRR 622
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDA--------AERELAQLQARLDSLERLQENLEGFSE 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-629 3.80e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  213 RELKTAKKKLVDMEHMVDELESEN-RNLTEKGRELKLIIDSLKsDVTNKRDTAKSSQQREQELSNILEEKEKESAQL--- 288
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKeKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKELESLegs 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  289 -------LQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRM 361
Cdd:PRK03918 254 krkleekIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI-EKRLSRLEEEINGIEERIKE 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  362 ATNENVDLEELLK---------GVTNGKAGLQFENNCLVGKLEEL-SFVSDRNKQDADNARAQLEEEREKHRLATEKLHQ 431
Cdd:PRK03918 333 LEEKEERLEELKKklkelekrlEELEERHELYEEAKAKKEELERLkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  432 EnIDYMKTSDSRIEMILEESKTRKMM------------DESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHL 499
Cdd:PRK03918 413 R-IGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  500 QKEGIQSVETYLQmakkrIEHLELELSATNA-TIEFQSQQLDRAGNMLIT-EQEIRNQTS-----VQYKERTSALENQLS 572
Cdd:PRK03918 492 ESELIKLKELAEQ-----LKELEEKLKKYNLeELEKKAEEYEKLKEKLIKlKGEIKSLKKeleklEELKKKLAELEKKLD 566
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660  573 QKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGK 629
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
393-630 7.83e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 7.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 393 KLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYM--KTSDSRIEMILEESKTRKMMDESTIERLRLDLD 470
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIARLEERRRELEERLEELEEELA 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 471 NEKSYKKNLEDLLNDLNQRALNSEMA-NHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITE 549
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 550 QEIRN--QTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:COG1196 407 EAEEAllERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                ...
gi 17539660 628 GKK 630
Cdd:COG1196 487 AEA 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
210-622 9.43e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 9.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLL 289
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 290 QQLEESRAALRDEQRHLEhqeaengkivEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDL 369
Cdd:COG4717 195 QDLAEELEELQQRLAELE----------EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGL 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 370 EELLKGVTNGKAGLQFennCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILE 449
Cdd:COG4717 265 GGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 450 esktrkmmdestierLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELElsatn 529
Cdd:COG4717 342 ---------------LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK----- 401
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 530 ATIEFQSQQLDRAGNMLITEQEIRNQTSV-----QYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE-SELKEQHEQL 603
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEEELeeeleELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEEL 481
                       410
                ....*....|....*....
gi 17539660 604 nvhhqsQQKLHSEAEKLRR 622
Cdd:COG4717 482 ------KAELRELAEEWAA 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-631 1.60e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    261 RDTAKSSQQREQELSNiLEEKEKESAQLLQQLEESRAALRDEQRHLEHQeaengkiVEQLKTVSElnekltmQVKDLQDA 340
Cdd:TIGR02168  666 AKTNSSILERRREIEE-LEEKIEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELE-------ELSRQISA 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    341 SENELASFRQKEKELIDELRMATNENVDLEELlkgvtngKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEERE 420
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    421 KHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDES--TIERLRLDLdneKSYKKNLEDLlnDLNQRALNSEmANH 498
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDI---ESLAAEIEEL--EELIEELESE-LEA 877
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    499 LQKEgIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLiteqeirnqtsVQYKERTSALENQLSQKDAEI 578
Cdd:TIGR02168  878 LLNE-RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-----------AQLELRLEGLEVRIDNLQERL 945
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17539660    579 ENLKRDLQQLVTKHESELKEqheqlnvhhqSQQKLHSEAEKLRREHEALGKKN 631
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIED----------DEEEARRRLKRLENKIKELGPVN 988
PTZ00121 PTZ00121
MAEBL; Provisional
219-630 1.71e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   219 KKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAA 298
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   299 lrdeqRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEELLKGVTN 378
Cdd:PTZ00121 1394 -----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   379 GKAGLQFENNC-LVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMM 457
Cdd:PTZ00121 1469 AKKADEAKKKAeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   458 DE-STIERLRLDLDNEKSYKKNLEDllNDLNQRALNSEMANHLQKEGIQSV-ETYLQMAKKRIEHLELELSATNATIEFQ 535
Cdd:PTZ00121 1549 DElKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   536 SQQLDRAGNMLIT---EQEIRNQTSVQYKERTSALENQLSQKDAEIEnlKRDLQQLvTKHESELKEQHEQLNVHHQSQQK 612
Cdd:PTZ00121 1627 KAEEEKKKVEQLKkkeAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEA-KKAEEDEKKAAEALKKEAEEAKK 1703
                         410
                  ....*....|....*...
gi 17539660   613 lhseAEKLRREHEALGKK 630
Cdd:PTZ00121 1704 ----AEELKKKEAEEKKK 1717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
268-628 2.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 268 QQREQELSNILEEKEKEsaqlLQQLE-ESRAA-----LRDEQRHLEHQEAengkiVEQLKTVSELNEKLTMQVKDLQDAS 341
Cdd:COG1196 185 EENLERLEDILGELERQ----LEPLErQAEKAeryreLKEELKELEAELL-----LLKLRELEAELEELEAELEELEAEL 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 342 ENELASFRQKEKElIDELRMA-TNENVDLEELLKgvtngkaglqfENNCLVGKLEELSFVSDRNKQDADNARAQLEEERE 420
Cdd:COG1196 256 EELEAELAELEAE-LEELRLElEELELELEEAQA-----------EEYELLAELARLEQDIARLEERRRELEERLEELEE 323
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 421 KHRLATEKLHQEnidymKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQ 500
Cdd:COG1196 324 ELAELEEELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 501 KEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmlITEQEIRNQTSVQYKERTSALENQLSQKDAEIEN 580
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE----EEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 17539660 581 LKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALG 628
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
PRK01156 PRK01156
chromosome segregation protein; Provisional
239-605 6.32e-08

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 56.45  E-value: 6.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  239 LTEKGRELKLIIDSLKSDVTNK---RDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENGK 315
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIdylEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  316 IVEQLKTVSELNEKLTMQVKDLQDASE--NELASFRQKEKELIDELRMATNENV--------DLEELLKGVTNGKAGLQ- 384
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEknNYYKELEERHMKIINDPVYKNRNYIndyfkyknDIENKKQILSNIDAEINk 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  385 FENNclVGKLEEL-SFVSD-----RNKQDADNARAQLEE-----------------EREKHRLATEKLHQENIDYMKTSD 441
Cdd:PRK01156 324 YHAI--IKKLSVLqKDYNDyikkkSRYDDLNNQILELEGyemdynsylksieslkkKIEEYSKNIERMSAFISEILKIQE 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  442 ---SRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRI 518
Cdd:PRK01156 402 idpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRL 481
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  519 E----HLELELSATNATIEFQSQQLDRagnmlITEQEIRnqtsvqykeRTSALENQLSQKDAEIENLKRDLQQLVTKHE- 593
Cdd:PRK01156 482 EekirEIEIEVKDIDEKIVDLKKRKEY-----LESEEIN---------KSINEYNKIESARADLEDIKIKINELKDKHDk 547
                        410
                 ....*....|...
gi 17539660  594 -SELKEQHEQLNV 605
Cdd:PRK01156 548 yEEIKNRYKSLKL 560
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
210-629 7.36e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 7.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLL 289
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 290 QQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDE---LRMATNEN 366
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarLLLLLEAE 500
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 367 VDLEELLKGVtnGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEERekhRLATEKLHQENIDYMKTSDS---- 442
Cdd:COG1196 501 ADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI---VVEDDEVAAAAIEYLKAAKAgrat 575
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 443 --RIEMILEESKTRKMMDESTIERLRLDLDNEKSY----KKNLEDLLNDLNQRALNSEMANHLQKE----------GIQS 506
Cdd:COG1196 576 flPLDKIRARAALAAALARGAIGAAVDLVASDLREadarYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEG 655
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 507 VETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQ 586
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 17539660 587 QLVTKHESELKEQHEQLNVHHQ---SQQKLHSEAEKLRREHEALGK 629
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIEALGP 781
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
213-627 8.70e-08

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: 56.23  E-value: 8.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    213 RELKTAKKKLVDMEHMVDELeSENRNLTEKGRELKLIIDSLKSdvtnkrdtakssQQREQELSNILEEKEKESAQLlQQL 292
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEK-RQQLERLRREREKAERYQALLK------------EKREYEGYELLKEKEALERQK-EAI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    293 EESRAALRDEQRHLEHQEAENGK-IVEQLKTVSELNEKLtmqvkdlQDASENELASFRQKEKELIDELRMatnenvdlee 371
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKrLEEIEQLLEELNKKI-------KDLGEEEQLRVKEKIGELEAEIAS---------- 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    372 llkgvtngkaglqfenncLVGKLEElsfvSDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsdsriemilees 451
Cdd:TIGR02169  306 ------------------LERSIAE----KERELEDAEERLAKLEAEIDKLLAEIEELERE------------------- 344
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    452 ktrkmmdestIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNAT 531
Cdd:TIGR02169  345 ----------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    532 IEFQSQQLdragnmliteQEIRNQTSVQyKERTSALENQLSQKDAEIENLKRDLQQLVTKHESElKEQHEQLNvhhQSQQ 611
Cdd:TIGR02169  415 LQRLSEEL----------ADLNAAIAGI-EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-EQELYDLK---EEYD 479
                          410
                   ....*....|....*.
gi 17539660    612 KLHSEAEKLRREHEAL 627
Cdd:TIGR02169  480 RVEKELSKLQRELAEA 495
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
214-620 9.07e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 9.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLE 293
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  294 ESRAALrdeQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEnELASFRQKEKELIDELRMATNENVDLEELL 373
Cdd:PRK02224 332 ECRVAA---QAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDAPVDL 407
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  374 KGVTNGKAGLQFENNCLVGKLEELSfVSDRNKQDA--------------------------------DNARAQLEEEREK 421
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELE-ATLRTARERveeaealleagkcpecgqpvegsphvetieedRERVEELEAELED 486
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  422 HRLATEKLHQ--ENIDYMKTSDSRIEMILEESKT---RKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMA 496
Cdd:PRK02224 487 LEEEVEEVEErlERAEDLVEAEDRIERLEERREDleeLIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  497 NHLQKEGIQSVETYLQMAKKRIEHLElELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYK---ERTSALENQLSq 573
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFD- 644
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660  574 kDAEIENLKRDLQQLVTKHE------------------------------SELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:PRK02224 645 -EARIEEAREDKERAEEYLEqveekldelreerddlqaeigaveneleelEELRERREALENRVEALEALYDEAEEL 720
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
213-626 1.44e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLksDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4717  88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERLEELRELEEEL 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENG-KIVEQLKTVSELNEKLTMQVKDLQDA---SENELASFRQKEKELIDELRMAT-NENV 367
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEEleeAQEELEELEEELEQLENELEAAAlEERL 245
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 368 DLEELLKGVTNGKAGLQFENNCLVGKLEE--------------LSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 434 IDYMKTSDSRIEMILEesktrkmmdestierLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQM 513
Cdd:COG4717 326 AALGLPPDLSPEELLE---------------LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 514 AKKRIEHLELElsatnATIEFQSQQLDRAGNmliteqEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE 593
Cdd:COG4717 391 LEQAEEYQELK-----EELEELEEQLEELLG------ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
                       410       420       430
                ....*....|....*....|....*....|...
gi 17539660 594 SELkEQHEQLNVHHQSQQKLHSEAEKLRREHEA 626
Cdd:COG4717 460 AEL-EQLEEDGELAELLQELEELKAELRELAEE 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
462-627 1.66e-07

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: 54.38  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 462 IERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDR 541
Cdd:COG4942  36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 542 AGNMlITEQEIRNQTSVQYKERTSALENQLSQKDAE-IENLKRDLQQLVTKhESELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:COG4942 116 LGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEAL 193

                ....*..
gi 17539660 621 RREHEAL 627
Cdd:COG4942 194 KAERQKL 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
214-679 2.21e-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: 54.64  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   214 ELKTAKKKLVDMEHMVDELESENrnltEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLE 293
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKI----QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   294 ESRAALRDEQRHLEHQeaeNGKIVEQLKTVSELNekltMQVKDLQDASENELasfrqkEKELIDELRMATNENVDLEELL 373
Cdd:TIGR04523 264 KIKKQLSEKQKELEQN---NKKIKELEKQLNQLK----SEISDLNNQKEQDW------NKELKSELKNQEKKLEEIQNQI 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   374 KgvtngkaglqfENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDY------MKTSDSRIEMI 447
Cdd:TIGR04523 331 S-----------QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYkqeiknLESQINDLESK 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   448 LEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSA 527
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   528 TNATIEFQSQQLDRAGNMLIT--------EQEIRNQTSVQ--YKERTSALENQLSQKDAEIENLKRDLQqlvtKHESELK 597
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKlneekkelEEKVKDLTKKIssLKEKIEKLESEKKEKESKISDLEDELN----KDDFELK 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   598 EqhEQLNVHHQSQQKlhsEAEKLRREHEALGKKNCFLGERCKIF---VKDSRSGVMKRSTSSDSLAEFLSKGN-DNETLE 673
Cdd:TIGR04523 556 K--ENLEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELIDQKekeKKDLIKEIEEKEKKISSLEKELEKAKkENEKLS 630

                  ....*.
gi 17539660   674 EMMRLI 679
Cdd:TIGR04523 631 SIIKNI 636
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
212-432 3.50e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQ 291
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKtvsELNEKLTMQVKDLQDASEnELASFRQKEKELIDELRMATNENVDLEE 371
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEE 407
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 372 LLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQE 432
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
231-623 4.37e-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: 53.92  E-value: 4.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    231 ELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQE 310
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    311 AENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKE-KELIDELRMATNENVDLEELLkgvtngkaglqfenNC 389
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL--------------RE 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    390 LVGKLEELSFvsdrnkqdadnARAQLEEEREKhrlateklhqenidymktsdsrIEMILEESKTRKMMDESTIERLRLDL 469
Cdd:TIGR02169  817 IEQKLNRLTL-----------EKEYLEKEIQE----------------------LQEQRIDLKEQIKSIEKEIENLNGKK 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    470 DNEKSYKKNLEDLLNDLNQR--ALNSEMANHlqKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLI 547
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRlgDLKKERDEL--EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660    548 TEQEIRNQTSV--QYKERTSALENQLsQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:TIGR02169  942 EDEEIPEEELSleDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
282-623 1.29e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  282 EKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSEL-------NEKLTMQVKDLQDASENELASFRQKEkE 354
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVleeheerREELETLEAEIEDLRETIAETERERE-E 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  355 LIDELRMATNENVDLEEllkgvtngkaglqfENNCLVGKLE----ELSFVSDRnKQDADNARAQLEEEREKHRLATEKlH 430
Cdd:PRK02224 277 LAEEVRDLRERLEELEE--------------ERDDLLAEAGlddaDAEAVEAR-REELEDRDEELRDRLEECRVAAQA-H 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  431 QENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETY 510
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  511 LQMAKKRIEHLELELSATNATIEfQSQQLDRAGNMLITEQEIRNQTSV----QYKERTSALENQLSQKDAEIENL----- 581
Cdd:PRK02224 421 RDELREREAELEATLRTARERVE-EAEALLEAGKCPECGQPVEGSPHVetieEDRERVEELEAELEDLEEEVEEVeerle 499
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  582 ------------------KRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:PRK02224 500 raedlveaedrierleerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
212-584 1.40e-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: 51.99  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQL--- 288
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELear 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    289 LQQLEESRAALRDEQRHLEHQEAEngkivEQLKTVSELNEKLTMQVKDLqdasENELASFRQKEKELIDELRMATNENVD 368
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    369 LEELLKGVTNGKAGLQFENNCLVGKLEElsfvsdrnkqdadnaraqLEEEREKHRLATEKLHQENIDyMKTSDSRIEMIL 448
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEE------------------LEEELEELEAALRDLESRLGD-LKKERDELEAQL 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    449 EESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNqralnsemANHLQKEGIQSVETYLQMAKKRIEHLELELSAt 528
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE--------DPKGEDEEIPEEELSLEDVQAELQRVEEEIRA- 969
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660    529 natiefqsqqLDRAGNMLITEQEIRNQTSVQYKERTSALE---NQLSQKDAEIENLKRD 584
Cdd:TIGR02169  970 ----------LEPVNMLAIQEYEEVLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
237-542 1.43e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 237 RNLTEKGRELKLI-----IDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEA 311
Cdd:COG1196 216 RELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 312 ENGKIVEQLKTVSELNEKLTMQVKDLQ---DASENELASFRQKEKELIDELRMATNENVDLEELLKGVtngkaglqfenn 388
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------ 363
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 389 clvgKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENidymktsdsrIEMILEESKTRKMMDESTIERLRLD 468
Cdd:COG1196 364 ----EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE----------LEEAEEALLERLERLEEELEELEEA 429
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539660 469 LDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRA 542
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
219-627 4.96e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   219 KKKLVDMEHMVDELESENRNLTEKGR----ELKLIIDSlKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKlqdeNLKELIEK-KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   295 SRAALRDEqrhLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELA----SFRQKEKELIDELRMATNENVDLE 370
Cdd:pfam05483 332 EKEAQMEE---LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   371 ElLKGVTNGKAGLQFENNC-------LVGKLEELSFVSDRNKQDADNARAQL------------EEEREKHRLATEKLhq 431
Cdd:pfam05483 409 E-LKKILAEDEKLLDEKKQfekiaeeLKGKEQELIFLLQAREKEIHDLEIQLtaiktseehylkEVEDLKTELEKEKL-- 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   432 ENIDYMKTSDsrieMILEESKtrKMMDESTIERLRLdldneksyKKNLEDLLNDLNQralnsEMANHLQKEGIQSVETYL 511
Cdd:pfam05483 486 KNIELTAHCD----KLLLENK--ELTQEASDMTLEL--------KKHQEDIINCKKQ-----EERMLKQIENLEEKEMNL 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   512 qmaKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTK 591
Cdd:pfam05483 547 ---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 17539660   592 HESELKeqheQLNVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:pfam05483 624 GSAENK----QLNAYEIKVNKLELELASAKQKFEEI 655
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
328-625 9.12e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.35  E-value: 9.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    328 EKLTMQVKDLQDA--SENELAS-----FRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFV 400
Cdd:pfam15921   81 EEYSHQVKDLQRRlnESNELHEkqkfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    401 SDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKN-- 478
Cdd:pfam15921  161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGri 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    479 --LEDLLndlnqRALNSEMANhlqkegiqSVETYLQMAKKRIEHL----ELELSA-TNATIEFQSQQLDRAGNMLITEQE 551
Cdd:pfam15921  241 fpVEDQL-----EALKSESQN--------KIELLLQQHQDRIEQLisehEVEITGlTEKASSARSQANSIQSQLEIIQEQ 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    552 IRNQTSVqYKERTSALENQLSQKDAEIENLKR-------DLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKL---- 620
Cdd:pfam15921  308 ARNQNSM-YMRQLSDLESTVSQLRSELREAKRmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladl 386

                   ....*.
gi 17539660    621 -RREHE 625
Cdd:pfam15921  387 hKREKE 392
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
214-648 9.48e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.58  E-value: 9.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKS------DVTNKRDTAKSSQQREQELSNILEEKEKESAQ 287
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    288 LLQQLEES----RAALRDEQRHLEHQEAE---NGKIVEQLKTVSELNEKLTmqvkdLQDASENELASFRQKEKELIDELR 360
Cdd:TIGR00618  516 ARQDIDNPgpltRRMQRGEQTYAQLETSEedvYHQLTSERKQRASLKEQMQ-----EIQQSFSILTQCDNRSKEDIPNLQ 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    361 matNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTS 440
Cdd:TIGR00618  591 ---NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    441 DSRIEMILEESKTRKMMDESTIERLRLD---LDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKR 517
Cdd:TIGR00618  668 RVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    518 IEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIEN-LKRDLQQL---VTKHE 593
Cdd:TIGR00618  748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeIPSDEDILnlqCETLV 827
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660    594 SELKEQHEQLNVHHQSQ----QKLHSEAEKLRREHEALGKKNCFLGERCKIFVKDSRSG 648
Cdd:TIGR00618  828 QEEEQFLSRLEEKSATLgeitHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKI 886
mukB PRK04863
chromosome partition protein MukB;
213-620 1.03e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   213 RELKTAKKKLVDMEH----MVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQRE--QELSNILEEKEKESA 286
Cdd:PRK04863  293 RELYTSRRQLAAEQYrlveMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAdlEELEERLEEQNEVVE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   287 QLLQQLEESRAALR--------------DEQRHLEHQEAENGKI---VEQLKTVSELNEKLTMQVKDLQDAseneLASFR 349
Cdd:PRK04863  373 EADEQQEENEARAEaaeeevdelksqlaDYQQALDVQQTRAIQYqqaVQALERAKQLCGLPDLTADNAEDW----LEEFQ 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   350 QKEKELIDELRMATNENVDLEEllkgvtngkAGLQFENNC-LVGKLeelsfVSDRNKQDADNARAQLEEEREKHRLATEK 428
Cdd:PRK04863  449 AKEQEATEELLSLEQKLSVAQA---------AHSQFEQAYqLVRKI-----AGEVSRSEAWDVARELLRRLREQRHLAEQ 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   429 LHQenidymktsdsrIEMILEEsktrkmmdestierLRLDLDNEksykKNLEDLLNDLNQRAlnsemanHLQKEGIQSVE 508
Cdd:PRK04863  515 LQQ------------LRMRLSE--------------LEQRLRQQ----QRAERLLAEFCKRL-------GKNLDDEDELE 557
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   509 TYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQL 588
Cdd:PRK04863  558 QLQEELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQL 636
                         410       420       430
                  ....*....|....*....|....*....|..
gi 17539660   589 VTkHESELKEQHEQLNvhhQSQQKLHSEAEKL 620
Cdd:PRK04863  637 LE-RERELTVERDELA---ARKQALDEEIERL 664
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
265-626 1.07e-05

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: 48.97  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   265 KSSQQREQElsnilEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQvkdlqdaSENE 344
Cdd:pfam17380 282 KAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-------RERE 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   345 LASFRQKEKElidelrmATNENVDLEELLKGVTNGKaglqfennclvgKLEELSF----VSDRNKQDADNARAQ--LEEE 418
Cdd:pfam17380 350 LERIRQEERK-------RELERIRQEEIAMEISRMR------------ELERLQMerqqKNERVRQELEAARKVkiLEEE 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   419 REKhRLATEKLHQENIDYMKTSDSRIEM-ILEESKTRKMmdestiERLRLDldnEKSYKKNLEDLLNDLNQRAlnsemAN 497
Cdd:pfam17380 411 RQR-KIQQQKVEMEQIRAEQEEARQREVrRLEEERAREM------ERVRLE---EQERQQQVERLRQQEEERK-----RK 475
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   498 HLQKEGIQSVETYLQMAKKRIEHLELElSATNATIEFQsqqldRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKdaE 577
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEE-----RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ--E 547
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17539660   578 IENLKRDLQQL--VTKHESELKEQHEQLNVHHQSQqklhsEAEKLRREHEA 626
Cdd:pfam17380 548 MEERRRIQEQMrkATEERSRLEAMEREREMMRQIV-----ESEKARAEYEA 593
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
215-618 1.59e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.89  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    215 LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:TIGR00606  704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    295 SRAALRDEqrhlehqeaengKIVEQLKTVSELNEKLTMQVKDLQDASENELA--SFRQKEKELIDELRMATNENVDLEEL 372
Cdd:TIGR00606  784 AKVCLTDV------------TIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqQVNQEKQEKQHELDTVVSKIELNRKL 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    373 LKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENID--YMKTSDSRIEMILEE 450
Cdd:TIGR00606  852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetFLEKDQQEKEELISS 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    451 SKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANhlqkegIQSVETYLQMAKKRIEHLELELSATNA 530
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE------LNTVNAQLEECEKHQEKINEDMRLMRQ 1005
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    531 TIEFQSQQlDRAGNMLITEQEIRNQTSVQYKERTSAL----ENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEqlnvh 606
Cdd:TIGR00606 1006 DIDTQKIQ-ERWLQDNLTLRKRENELKEVEEELKQHLkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKG----- 1079
                          410
                   ....*....|..
gi 17539660    607 hQSQQKLHSEAE 618
Cdd:TIGR00606 1080 -YEKEIKHFKKE 1090
PLN02939 PLN02939
transferase, transferring glycosyl groups
251-625 1.76e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 48.36  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  251 DSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRH----LEHQEAENGKIVEQLKTVSEL 326
Cdd:PLN02939  43 SSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHnrasMQRDEAIAAIDNEQQTNSKDG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  327 NEKLTMQVKDLQDASENElasfrQKEKELIDELRMATNEnvDLEELLKGvtngKAGLQFENNCLVGKLEEL---SFVSDR 403
Cdd:PLN02939 123 EQLSDFQLEDLVGMIQNA-----EKNILLLNQARLQALE--DLEKILTE----KEALQGKINILEMRLSETdarIKLAAQ 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  404 NKQDADNARAQLEEEREK--HRLATEKlhqenidymkTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLED 481
Cdd:PLN02939 192 EKIHVEILEEQLEKLRNEllIRGATEG----------LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  482 LLNdlnQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSvqyK 561
Cdd:PLN02939 262 LEK---ERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVD---K 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660  562 ERTSALENQLSQKDAE-IENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHE 625
Cdd:PLN02939 336 LEASLKEANVSKFSSYkVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
214-630 2.25e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKliidSLKSDVTNKRDTAKSSQQREQELSNILEEKEKesaqllqqLE 293
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSR--------LE 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  294 ESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDAS--ENELASFRQKEK-----ELIDELRMATNEN 366
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakKEELERLKKRLTgltpeKLEKELEELEKAK 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  367 VDLEELLKGVTNGKAGLQFENNCLVGKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQENIDY-MKTSDSRIE 445
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEEL----KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKER 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  446 MILEESKT--RKMMDESTIERLRLDLD-----NEKSYKKNLEDLLNDLNQRALNSEMANHLQKE---------GIQSVET 509
Cdd:PRK03918 477 KLRKELREleKVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikslkkeleKLEELKK 556
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  510 YLQMAKKRIEHLELELSATNATIE---FQS--------QQLDRAGNMLIT----EQEIRNQTSVQYKERT--SALENQLS 572
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEelgFESveeleerlKELEPFYNEYLElkdaEKELEREEKELKKLEEelDKAFEELA 636
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660  573 QKDAEIENLKRDLQQL---------------VTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:PRK03918 637 ETEKRLEELRKELEELekkyseeeyeelreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
268-630 2.57e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.79  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   268 QQREQELSNILEEKEKESAQLLQQLEESRAALRD------EQRHLEHQEAENGKIV-EQLKTVSELNEKLTMQVKDLQDA 340
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMS 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   341 SENELASfrqkEKELIDELRMATNENVDL----EELLKGVTNGKAGLQF---ENNCLVGKLEELSfvsdRNKQDadnara 413
Cdd:pfam05483 305 LQRSMST----QKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFvvtEFEATTCSLEELL----RTEQQ------ 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   414 QLEEEREKHRLATEKLHQEN--IDYMKTSDSRIEMILEESKT-----RKMMDES-TIERLRLDLDNE--------KSYKK 477
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSseLEEMTKFKNNKEVELEELKKilaedEKLLDEKkQFEKIAEELKGKeqelifllQAREK 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   478 NLEDLLNDLNQRALNSE--------MANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGN----- 544
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEhylkevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkkqee 530
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   545 MLITEQEIRNQTSVQYKERTSALENQLSQKDAEI-------ENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEA 617
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
                         410
                  ....*....|...
gi 17539660   618 EKLRREHEALGKK 630
Cdd:pfam05483 611 EELHQENKALKKK 623
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
237-620 2.74e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.02  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  237 RNLTEKGRELKLIIDsLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEaengKI 316
Cdd:COG3096  275 RHANERRELSERALE-LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE----KI 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  317 VEQLKTVSELNEKL---TMQVKDLQDASENELASFRQKEKElIDELRmatNENVDLEELLKgVTNGKAgLQFENncLVGK 393
Cdd:COG3096  350 ERYQEDLEELTERLeeqEEVVEEAAEQLAEAEARLEAAEEE-VDSLK---SQLADYQQALD-VQQTRA-IQYQQ--AVQA 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  394 LEELSFVSDRNKQDADNARAQLEEEREKHRLATEKL--HQENIDYMKTSDSRIEMILEesKTRKMMDE-----------S 460
Cdd:COG3096  422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleLEQKLSVADAARRQFEKAYE--LVCKIAGEversqawqtarE 499
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  461 TIERLRlDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAkkriEHLELELSATNATIEFQSQQLD 540
Cdd:COG3096  500 LLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELEAQLEELEEQAA 574
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  541 RAGNMLITEQEIRNQTSVQYKE-------------RTSALENQLSQKDAEIENLKRDLQQLVtKHESELKEQHEQLNvhh 607
Cdd:COG3096  575 EAVEQRSELRQQLEQLRARIKElaarapawlaaqdALERLREQSGEALADSQEVTAAMQQLL-EREREATVERDELA--- 650
                        410
                 ....*....|...
gi 17539660  608 QSQQKLHSEAEKL 620
Cdd:COG3096  651 ARKQALESQIERL 663
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
406-603 3.08e-05

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: 46.07  E-value: 3.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 406 QDADNARAQLEEEREKHRLATEKLhQENIDYMKTSDSRIEMILEESKTRkmmdestIERLRLDLDNEKSYKKNLEDLLNd 485
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAEL-EDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEARIKKYEEQLG- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 486 lnqRALNSEMANHLQKEgiqsvetyLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmliteQEIRNQTSVQYKERTS 565
Cdd:COG1579  84 ---NVRNNKEYEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKA 145
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17539660 566 ALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQL 603
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLALYERI 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
207-588 7.15e-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: 7.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 207 KYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESA 286
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 287 QLLQQLEESRAALRDEQRHLEHQEA-ENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMAT-- 363
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAArLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaa 546
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 364 ---NENVDLE-------ELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG1196 547 alqNIVVEDDevaaaaiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 434 IDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVEtyLQM 513
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA--EEE 704
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 514 AKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQL 588
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
197-612 9.33e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   197 IAEVVDSPTMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQ---REQE 273
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEElkgKEQE 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   274 LSNILEEKEKESAQLLQQLEESRAA-------LRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQ---DASEN 343
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSeehylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlelKKHQE 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   344 ELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEE-------LSFVSDRNKQDADNARAQLE 416
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEnarsieyEVLKKEKQMKILENKCNNLK 600
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   417 EEREKHRLATEKLHQENIDYMKTSDSriemileESKTRKMMdESTIERLRLDLDNEK--------SYKKNLED------- 481
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSA-------ENKQLNAY-EIKVNKLELELASAKqkfeeiidNYQKEIEDkkiseek 672
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   482 LLNDLNQRALNSEMANHLQKEgiqsvetylqmAKKRIEHlelELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYK 561
Cdd:pfam05483 673 LLEEVEKAKAIADEAVKLQKE-----------IDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17539660   562 ERTSALENQLSQKDAEIENLKRDLQqlVTKHESELKEQHEQLNVHHQSQQK 612
Cdd:pfam05483 739 SAKAALEIELSNIKAELLSLKKQLE--IEKEEKEKLKMEAKENTAILKDKK 787
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
275-490 1.12e-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: 45.53  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 275 SNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAE----NGKIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQ 350
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAEL-EKEIAELRA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 351 KEKELIDEL--RMATNENVDLEELLKGVTNGKAGLQFENNclvgkLEELSFVSDRNKQDADNARAQLEEEREKHRLATEK 428
Cdd:COG4942  98 ELEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539660 429 LHQENIDYMKTSDSRIEMILEESKTRKMMD--ESTIERLRLDLDNEKSYKKNLEDLLNDLNQRA 490
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLArlEKELAELAAELAELQQEAEELEALIARLEAEA 236
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
228-621 1.30e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    228 MVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKssQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLE 307
Cdd:pfam15921  225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    308 H-QEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEnelaSFRQKEKELIDELRMATNEnvdleellkgvtngkaglqfe 386
Cdd:pfam15921  303 IiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR----MYEDKIEELEKQLVLANSE--------------------- 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    387 nnclvgkLEELSFVSDRNKQDADNARAQLEEerekhrlATEKLHQEnidymktsdsRIEMILEESKTRKMMDES-----T 461
Cdd:pfam15921  358 -------LTEARTERDQFSQESGNLDDQLQK-------LLADLHKR----------EKELSLEKEQNKRLWDRDtgnsiT 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    462 IERLRLDLDNEKSYKKNLEDLLndlnqRALNSEMANHLQKegiqsvetylQMAKKRIEHLELE-LSATNATIEFQSQQLD 540
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALL-----KAMKSECQGQMER----------QMAAIQGKNESLEkVSSLTAQLESTKEMLR 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    541 RagnmlITEQEIRNQTSVQYKERT-SALENQLSQKDAEIENLKRDLQQLVTKHESELKE-QHEQLNVHHQSQQKLHSEAE 618
Cdd:pfam15921  479 K-----VVEELTAKKMTLESSERTvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEAL 553

                   ...
gi 17539660    619 KLR 621
Cdd:pfam15921  554 KLQ 556
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
445-630 1.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  445 EMILEESKTRKMMDE-----STIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEG----IQSVETYLQMAK 515
Cdd:COG4913  215 EYMLEEPDTFEAADAlvehfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLE 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  516 KRIEHLELELSATNATIEFQSQQLDRAGNMLIT----------------EQEI---------RNQTSVQYKERTSALENQ 570
Cdd:COG4913  295 AELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdrleqlEREIerlereleeRERRRARLEALLAALGLP 374
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  571 LSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:COG4913  375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-630 1.55e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4913  338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  293 EESRAALRDEQRHLEHQ---------------EAENGKIVEQLKTVSELnekltMQVKDL----QDASENELASFR---- 349
Cdd:COG4913  418 RRELRELEAEIASLERRksniparllalrdalAEALGLDEAELPFVGEL-----IEVRPEeerwRGAIERVLGGFAltll 492
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  350 ------QKEKELIDELRMATNenVDLEELLKGVTNgKAGLQFENNCLVGKLE-----ELSFVSDRNKQDADNARAQLEEE 418
Cdd:COG4913  493 vppehyAAALRWVNRLHLRGR--LVYERVRTGLPD-PERPRLDPDSLAGKLDfkphpFRAWLEAELGRRFDYVCVDSPEE 569
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  419 REKHRLA-TE--------KLHQENIDYMKTSD--------SRIEMILEEsktrkmmdestIERLRLDLDNEKSYKKNLED 481
Cdd:COG4913  570 LRRHPRAiTRagqvkgngTRHEKDDRRRIRSRyvlgfdnrAKLAALEAE-----------LAELEEELAEAEERLEALEA 638
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  482 LLNDLNQRAlnsemANHLQKEGIQSVETYLQMAKKRIEHLELE---LSATNATIEFQSQQLDRAgnmlitEQEIR--NQT 556
Cdd:COG4913  639 ELDALQERR-----EALQRLAEYSWDEIDVASAEREIAELEAElerLDASSDDLAALEEQLEEL------EAELEelEEE 707
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  557 SVQYKERTSALENQLSQKDAEIENLKRDLQQLVTK----HESELKEQHEQL---NVHHQSQQKLHSEAEKLRREHEALGK 629
Cdd:COG4913  708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarleLRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEE 787

                 .
gi 17539660  630 K 630
Cdd:COG4913  788 E 788
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
229-631 1.74e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  229 VDELESENRNLTEKGRELKLIIDSLKSDVtnkrdtakssqQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEH 308
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  309 QEAEngkiVEQLKTVSELNEKLTMQVKDLqdasENELASFRQKEKELIDELRMATNENVDLEEllkgvtngkaglqfenn 388
Cdd:PRK03918 226 LEKE----VKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERIEELKKEIEELEE----------------- 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  389 cLVGKLEELsfvsdrnKQDADNARAqLEEEREKHRLATEKLHQENIDYMKTSDSRIEMI--LEESKTRKMMDESTIERLR 466
Cdd:PRK03918 281 -KVKELKEL-------KEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLKELE 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  467 LDLDNEKSYKKNLEDLlndlnqRALNSEMANHLQKEGIQSVET------YLQMAKKRIEHLELELSATNATIEFQSQQLD 540
Cdd:PRK03918 352 KRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKlekeleELEKAKEEIEEEISKITARIGELKKEIKELK 425
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  541 RAGNML--------ITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLnvhhqsqqK 612
Cdd:PRK03918 426 KAIEELkkakgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--------K 497
                        410
                 ....*....|....*....
gi 17539660  613 LHSEAEKLRREHEALGKKN 631
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYN 516
PTZ00121 PTZ00121
MAEBL; Provisional
213-630 2.00e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDT-----AKSSQQREQELSNILEEKEKeSAQ 287
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelkkAAAAKKKADEAKKKAEEKKK-ADE 1435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   288 LLQQLEESRAALRDEQRHLEHQEAEN-GKIVEQLKTVSELNEKLTMQVKdlqdasENELASFRQKEKELIDELRMATNEN 366
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADEAKKAAEAK 1509
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   367 VDLEELLKGVTNGKAGlQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYM--------K 438
Cdd:PTZ00121 1510 KKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakK 1588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   439 TSDSRIEMIL---EESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAK 515
Cdd:PTZ00121 1589 AEEARIEEVMklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   516 KRIEHLEL--ELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSvQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE 593
Cdd:PTZ00121 1669 KAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA-EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 17539660   594 SELKEQHEQLNVHHQSQQKlHSEAEKLRREHEALGKK 630
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEE 1783
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
459-627 2.36e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 459 ESTIERLRLDLDNEKSYKKNLEDLLNDLNQRAlnsemaNHLQKEgIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQ 538
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAEL------EELNEE-YNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 539 LD-------RAGNMLITEQEIRNQTSVQ-YKERTSALENQLSQKDAEIENLKRDLQQLVTKhESELKEQHEQLNVHHQSQ 610
Cdd:COG3883  88 LGeraralyRSGGSVSYLDVLLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAK-KAELEAKLAELEALKAEL 166
                       170
                ....*....|....*..
gi 17539660 611 QKLHSEAEKLRREHEAL 627
Cdd:COG3883 167 EAAKAELEAQQAEQEAL 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
212-487 4.58e-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: 43.86  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKsdvtnkrdtaKSSQQREQELSNILEEKEKESAQlLQQ 291
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----------KLNQQKDEQIKKLQQEKELLEKE-IER 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   292 LEESRAALRDEQRHLEHQEAENGKIVEQLKTvseLNEKLTMQVKDLQDASENELASFRQKEKEL---IDELRMATNENVD 368
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKIKQNLEQKQKELkskEKELKKLNEEKKE 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   369 LEELLKGVTNGKAGL-----QFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSR 443
Cdd:TIGR04523 508 LEEKVKDLTKKISSLkekieKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 17539660   444 IEMILEESKTRK------MMDESTIERLRLDLDNEKSYKKNLEDLLNDLN 487
Cdd:TIGR04523 588 QELIDQKEKEKKdlikeiEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
270-618 4.83e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   270 REQELSNILEEKEKESAQLLQ-------QLEESRAALRDEQRHLEHQEAENGKIVEQLKTV----SELNEKLTMQVKDLQ 338
Cdd:pfam07888  28 RAELLQNRLEECLQERAELLQaqeaanrQREKEKERYKRDREQWERQRRELESRVAELKEElrqsREKHEELEEKYKELS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   339 DASEnELAsfrqKEKELIDELRMATNENV-DLEELLKGVTNGKaglqfennclVGKLEELsfvsDRNKQDADNARAQLEE 417
Cdd:pfam07888 108 ASSE-ELS----EEKDALLAQRAAHEARIrELEEDIKTLTQRV----------LERETEL----ERMKERAKKAGAQRKE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   418 EREKHRLATEKLHQ--ENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDL--------- 486
Cdd:pfam07888 169 EEAERKQLQAKLQQteEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrslqerlna 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   487 NQR---ALNSEMAN----------HLQKEGIQSVETYLQMAKKRI-------------EHLELELSATNATIEFQSQQLD 540
Cdd:pfam07888 249 SERkveGLGEELSSmaaqrdrtqaELHQARLQAAQLTLQLADASLalregrarwaqerETLQQSAEADKDRIEKLSAELQ 328
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660   541 RAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAE 618
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
218-347 5.52e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 5.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 218 AKKKLvDMEHMVDELESenrnLTEKGRELKLIIDSLKsdvtnkRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRA 297
Cdd:COG0542 400 ARVRM-EIDSKPEELDE----LERRLEQLEIEKEALK------KEQDEASFERLAELRDELAELEEELEALKARWEAEKE 468
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17539660 298 ALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDA-SENELAS 347
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAE 519
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
288-631 5.86e-04

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: 43.81  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    288 LLQQLEESRAALRDEQRHLEHQEA-----ENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMA 362
Cdd:pfam02463  138 LVQGGKIEIIAMMKPERRLEIEEEaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    363 TNENVDLEELLKgvtnGKAGLQFENNCLVGKLEELSfvsdRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDS 442
Cdd:pfam02463  218 KLELEEEYLLYL----DYLKLNEERIDLLQELLRDE----QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    443 RIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLE 522
Cdd:pfam02463  290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    523 LELSATNATIEFQSQQLDRAGNMLITEQEIRNQtsvqyKERTSALENQLSQK---DAEIENLKRDLQQLVTKHESELKEQ 599
Cdd:pfam02463  370 QLEEELLAKKKLESERLSSAAKLKEEELELKSE-----EEKEAQLLLELARQledLLKEEKKEELEILEEEEESIELKQG 444
                          330       340       350
                   ....*....|....*....|....*....|..
gi 17539660    600 HEQLNVHHQSQQKLHSEAEKLRREHEALGKKN 631
Cdd:pfam02463  445 KLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
212-623 8.25e-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: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNIL-------EEKEKE 284
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILhelesrlEEEEER 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    285 SAQLLQQLEESRAALRDEQRHLEHQEAENGK--------------IVEQLKTVSELNEKLTMQVKDLQDaSENELASFRQ 350
Cdd:pfam01576   91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEE-RISEFTSNLA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    351 KEKELIDELRMATNEN----VDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:pfam01576  170 EEEEKAKSLSKLKNKHeamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    427 EKLHQENIDYMKTSDSRIEMileesktrkmmdESTIERLRLDLDNEKSYKKNLEDLLNDLNQ--RALNSEMANHL----- 499
Cdd:pfam01576  250 ARLEEETAQKNNALKKIREL------------EAQISELQEDLESERAARNKAEKQRRDLGEelEALKTELEDTLdttaa 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    500 QKEGIQSVETYLQMAKKRIEHlelELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIe 579
Cdd:pfam01576  318 QQELRSKREQEVTELKKALEE---ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL- 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 17539660    580 nlkRDLQQLVTKHESELKEQHEQLnvhhQSQQKLHSEAEKLRRE 623
Cdd:pfam01576  394 ---RTLQQAKQDSEHKRKKLEGQL----QELQARLSESERQRAE 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
213-452 1.35e-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: 42.06  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EesRAALRDEQRHLEHQEAENGKIveqlktvselneKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG4942 114 Y--RLGRQPPLALLLSPEDFLDAV------------RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAGLQfennclvgkleelsfvsdRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESK 452
Cdd:COG4942 180 LAELEEERAALE------------------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
344-617 1.42e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  344 ELASFRQKEKELIDELRmatNEN-VDLEELLKGVTNGKAGLQFENnclvgkLEELSFVSDRNKQDADNARAQLEEEREKH 422
Cdd:PRK05771  10 LIVTLKSYKDEVLEALH---ELGvVHIEDLKEELSNERLRKLRSL------LTKLSEALDKLRSYLPKLNPLREEKKKVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  423 RLATEKLHQEnidymktSDSRIEMILEESKtrkmmdeSTIERLRlDLDNEKsykKNLEDLLNDLNQ-RALNSEMANHLQK 501
Cdd:PRK05771  81 VKSLEELIKD-------VEEELEKIEKEIK-------ELEEEIS-ELENEI---KELEQEIERLEPwGNFDLDLSLLLGF 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  502 EGIqSVETYLqMAKKRIEHLELELSATNATIEFQSQQLDRAgnMLITEQEIRNQTSVQYK----------------ERTS 565
Cdd:PRK05771 143 KYV-SVFVGT-VPEDKLEELKLESDVENVEYISTDKGYVYV--VVVVLKELSDEVEEELKklgferleleeegtpsELIR 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17539660  566 ALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLnvhhqSQQKLHSEA 617
Cdd:PRK05771 219 EIKEELEEIEKERESLLEELKELAKKYLEELLALYEYL-----EIELERAEA 265
PRK12704 PRK12704
phosphodiesterase; Provisional
550-626 1.62e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  550 QEIRNQTSVQYKERTS---ALENQLSQKDaeiENLKRDLQQLvTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEA 626
Cdd:PRK12704  67 HKLRNEFEKELRERRNelqKLEKRLLQKE---ENLDRKLELL-EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
212-358 1.66e-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: 41.06  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQR----EQELSNILEEKEKESAQ 287
Cdd:COG1579  16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYEALQ 95
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539660 288 L-LQQLEESRAALRDEQRHLEHQEAEngkIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDE 358
Cdd:COG1579  96 KeIESLKRRISDLEDEILELMERIEE---LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
500-603 1.83e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 500 QKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmlitEQEIRNQTsvqykERTSALENQLSQKDAEIE 579
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL------ERRIAALA-----RRIRALEQELAALEAELA 86
                        90       100
                ....*....|....*....|....
gi 17539660 580 NLKRDLQQLvtkhESELKEQHEQL 603
Cdd:COG4942  87 ELEKEIAEL----RAELEAQKEEL 106
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
209-630 1.88e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    209 MRSDRE--LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQReqelsniLEEKEKESA 286
Cdd:pfam01576  188 MISDLEerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR-------LEEETAQKN 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    287 QLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQD--ASENELASFRQKEkelIDELRMATN 364
Cdd:pfam01576  261 NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDttAAQQELRSKREQE---VTELKKALE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    365 ENVDLEEllkgvtngkaglqfennclvgkleelsfvsdrnkqdadnarAQLEEEREKHRLATEKLhQENIDYMKTSDSRI 444
Cdd:pfam01576  338 EETRSHE-----------------------------------------AQLQEMRQKHTQALEEL-TEQLEQAKRNKANL 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    445 E---MILEESKTRKMMDESTIERLRLDLDNEKsykKNLEDLLNDLNQRALNSEMA--------NHLQKEgIQSVETYLQM 513
Cdd:pfam01576  376 EkakQALESENAELQAELRTLQQAKQDSEHKR---KKLEGQLQELQARLSESERQraelaeklSKLQSE-LESVSSLLNE 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    514 AKKRIEHLELELSATNATIEFQSQQLDRAgnmliTEQEIRNQTSV-QYKERTSALENQLSQKDAEIENLKRDLQQLvTKH 592
Cdd:pfam01576  452 AEGKNIKLSKDVSSLESQLQDTQELLQEE-----TRQKLNLSTRLrQLEDERNSLQEQLEEEEEAKRNVERQLSTL-QAQ 525
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 17539660    593 ESELKEQHEQLNvhhQSQQKLHSEAEKLRREHEALGKK 630
Cdd:pfam01576  526 LSDMKKKLEEDA---GTLEALEEGKKRLQRELEALTQQ 560
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
222-331 1.94e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 222 LVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRD 301
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
                        90       100       110
                ....*....|....*....|....*....|
gi 17539660 302 EQRHLEHQEAENGKIVEQLKTVSELNEKLT 331
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERT 243
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
215-623 2.03e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 42.13  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   215 LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:PTZ00440  765 LYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT 844
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   295 sraalrdeqrhlehqEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENelasfrqkeKELIDELRMATNENVDLEELLK 374
Cdd:PTZ00440  845 ---------------EDENLNLKELEKEFNENNQIVDNIIKDIENMNKN---------INIIKTLNIAINRSNSNKQLVE 900
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   375 GVTNGKAGL---------QFENNCLVGKLEELSFVSDRNKqdadnaraqlEEEREKHRLATEKLHQENIDymktsdsrIE 445
Cdd:PTZ00440  901 HLLNNKIDLknkleqhmkIINTDNIIQKNEKLNLLNNLNK----------EKEKIEKQLSDTKINNLKMQ--------IE 962
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   446 MILEESKTRKM----MDESTIERLRLDLDNEKSYKKNLEDLlnDLNQRALNSEMANHLQKEGIQSVETYLQMAK------ 515
Cdd:PTZ00440  963 KTLEYYDKSKEningNDGTHLEKLDKEKDEWEHFKSEIDKL--NVNYNILNKKIDDLIKKQHDDIIELIDKLIKekgkei 1040
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   516 -----KRIEHLElELSATNATIEFqSQQLDRAGNMLITEQEIrnqtsvQYKERTSALENQLSQKDAEIENLKRDLQQLVT 590
Cdd:PTZ00440 1041 eekvdQYISLLE-KMKTKLSSFHF-NIDIKKYKNPKIKEEIK------LLEEKVEALLKKIDENKNKLIEIKNKSHEHVV 1112
                         410       420       430
                  ....*....|....*....|....*....|...
gi 17539660   591 KHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:PTZ00440 1113 NADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKE 1145
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
266-630 2.22e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    266 SSQQREQELSNILEE--KEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEN 343
Cdd:TIGR00618  220 RKQVLEKELKHLREAlqQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    344 E-LASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEElsfvSDRNKQDADNARAQLEEEREKH 422
Cdd:TIGR00618  300 KaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ----EIHIRDAHEVATSIREISCQQH 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    423 RLaTEKLHQenidymktsdsriemiLEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKE 502
Cdd:TIGR00618  376 TL-TQHIHT----------------LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    503 GI----QSVETYLQMAKKRIEHLELELSATNATiEFQSQQLDRagnmlITEQEIRNQTSV------------QYKERTSA 566
Cdd:TIGR00618  439 YAelcaAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQ-----IHLQETRKKAVVlarllelqeepcPLCGSCIH 512
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660    567 LENQLSQKDaEIENLKRDLQQL---VTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:TIGR00618  513 PNPARQDID-NPGPLTRRMQRGeqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC 578
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
201-624 2.82e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    201 VDSPTMKYMRSDRELKTAKKKLV-DMEHMVDELESENRNLtEKGRELKLIIDSLKS-------DVTNKRDTAKSSQQREQ 272
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESL-EKVSSLTAQLESTKEmlrkvveELTAKKMTLESSERTVS 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    273 ELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENgkivEQLKTVSELNEKLTMQVkdlqdasenelasfrqKE 352
Cdd:pfam15921  500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG----DHLRNVQTECEALKLQM----------------AE 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    353 KELIDELRMATNENVDLEELLKGVTNG-----KAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEE-EREKHRLAT 426
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQHGRTAGamqveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVKLVN 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    427 EKlhQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQS 506
Cdd:pfam15921  640 AG--SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660    507 VETYLQMAKKRIEHLELELSATNATIE-FQS--QQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLK- 582
Cdd:pfam15921  718 MEGSDGHAMKVAMGMQKQITAKRGQIDaLQSkiQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRs 797
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 17539660    583 --RDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREH 624
Cdd:pfam15921  798 qeRRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQH 841
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
213-524 3.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLvdmEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQlLQQL 292
Cdd:COG4372  45 EELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-LEEL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAE-NGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEE 371
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAElQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 372 LLKGVTNGKAGLQFENnclvgKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEES 451
Cdd:COG4372 201 ELAEAEKLIESLPREL-----AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 452 KTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELE 524
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
214-429 3.43e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  214 ELKTAKKKLvdMEHMVDELESEN---RNLTEKGRELKLIIDSLKSDVTNKRDTAKssqqREQELSNILEEKEKESAQLLQ 290
Cdd:PRK03918 504 QLKELEEKL--KKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEELAELLK 577
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  291 QLEE-SRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLtmqvkDLQDASENELASFRQKEKELIDELRMATNENVDL 369
Cdd:PRK03918 578 ELEElGFESVEELEERLKELEPFYNEYLELKDAEKELEREE-----KELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660  370 -----EELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLeEEREKHRLATEKL 429
Cdd:PRK03918 653 ekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKL 716
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
231-374 3.63e-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: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 231 ELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALR-----DEQRH 305
Cdd:COG1579  14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKEYEA 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 306 LEHQEAENGKIVEQL-KTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRMATNE-NVDLEELLK 374
Cdd:COG1579  94 LQKEIESLKRRISDLeDEILELMERIEELEEELAEL-EAELAELEAELEEKKAELDEELAElEAELEELEA 163
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
511-623 4.82e-03

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 40.13  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   511 LQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQyKERTSALENQLSQ-------KDAEIENLKR 583
Cdd:pfam10186  28 LARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLLKSEVAIS-NERLNEIKDKLDQlrreiaeKKKKIEKLRS 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17539660   584 DLQQLVTKHES---ELKE-QHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:pfam10186 107 SLKQRRSDLESasyQLEErRASQLAKLQNSIKRIKQKWTALHSK 150
PTZ00121 PTZ00121
MAEBL; Provisional
198-525 5.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   198 AEVVDSPTMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQqREQELSNI 277
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKI 1661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   278 LEEKEKESAQL-LQQLEESRAALRDEQRHLE--HQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKE 354
Cdd:PTZ00121 1662 KAAEEAKKAEEdKKKAEEAKKAEEDEKKAAEalKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   355 ---LIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLV-----GKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:PTZ00121 1742 dkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeldEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   427 EKLHQENIDYMKTSDSRIEMILEESKtrkmmdesTIERLRLDLDNEKSYKKNLE-------DLLNDLNQRALNSEMANHL 499
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEAD--------AFEKHKFNKNNENGEDGNKEadfnkekDLKEDDEEEIEEADEIEKI 1893
                         330       340
                  ....*....|....*....|....*.
gi 17539660   500 QKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:PTZ00121 1894 DKDDIEREIPNNNMAGKNNDIIDDKL 1919
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
205-488 5.21e-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: 40.39  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   205 TMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSdvtnkrdtakssqqREQELSNILEEKEKE 284
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE--------------KIEKLESEKKEKESK 539
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   285 SAQLLQQLEESRAALRDEQrhLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASE-------NELASFRQKEKELID 357
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEkekkdliKEIEEKEKKISSLEK 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   358 ELRMATNENVDLEELLKGVTNGKAGLQfennclvgklEELSFVsdrnKQDADNARAQLEEEREKHRLATEKLhQENIDYM 437
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKNKLK----------QEVKQI----KETIKEIRNKWPEIIKKIKESKTKI-DDIIELM 682
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660   438 KTSDSRIEMILEESKTRKMMD------ESTIERLRLDLDNEKSYKKNLEDLLNDLNQ 488
Cdd:TIGR04523 683 KDWLKELSLHYKKYITRMIRIkdlpklEEKYKEIEKELKKLDEFSKELENIIKNFNK 739
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
214-647 5.57e-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: 40.39  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKssqQREQELSNILEE----------KEK 283
Cdd:TIGR04523  48 ELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN---KLNSDLSKINSEikndkeqknkLEV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   284 ESAQLLQQLEESRAALRDEQRHLEHQEAE----NGKIVEQLKTVSELNEKLTMQVKDLQDASEN---------------- 343
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKNidkiknkllklellls 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   344 ELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHR 423
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   424 LATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEG 503
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   504 IQSVETYLQMAKKR-------IEHLELELSATNATIEFQSQQ----------LDRAGNMLITEQEIRNQTSVQYKERTSA 566
Cdd:TIGR04523 365 LEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLnqqkdeqikkLQQEKELLEKEIERLKETIIKNNSEIKD 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660   567 LENQLSQKDAEIENLKRDLQQLvtkhESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKKNCFLGERCKIFVKDSR 646
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESL----ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520

                  .
gi 17539660   647 S 647
Cdd:TIGR04523 521 S 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
402-630 5.95e-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: 39.75  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 402 DRNKQDADNARAQLEEEREKHRLATEKL--HQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKsykKNL 479
Cdd:COG4942  30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EEL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 480 EDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEfqsqQLDRAGNMLITEQEIRNQTSVQ 559
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAE 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 560 YKERTSALENQLSQKdaeienlkrdlQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:COG4942 183 LEEERAALEALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
479-627 6.36e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 479 LEDLLNDLNQRALNSE--MANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEI---- 552
Cdd:COG3206 180 LEEQLPELRKELEEAEaaLEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 553 -RNQTSVQYKERTSALENQLSQK--------------DAEIENLKRDLQQLVTK--------------HESELKEQHEQL 603
Cdd:COG3206 260 lQSPVIQQLRAQLAELEAELAELsarytpnhpdvialRAQIAALRAQLQQEAQRilasleaelealqaREASLQAQLAQL 339
                       170       180
                ....*....|....*....|....
gi 17539660 604 NVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEVA 363
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
233-433 6.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 233 ESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEA- 311
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARa 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 312 --ENGKIVEQL------KTVSELNEKLTMqVKDLQDASENELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGL 383
Cdd:COG3883  95 lyRSGGSVSYLdvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17539660 384 QfennclvGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG3883 174 E-------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
219-508 7.08e-03

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.


Pssm-ID: 185749 [Multi-domain]  Cd Length: 353  Bit Score: 39.65  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 219 KKKLVDmEHMVDELESENRNLTEKGRELKL--IIDSLKSDVTNKRDTAKSSQQREQE-----LSNILEEKEKESAQLLQQ 291
Cdd:cd09236  15 KDRLVN-ESIIDELEELTNRAHSTLRSLNLpgSLQALEKPLGLPPSLLRHAEEIRQEdglerIRASLDDVARLAASDRAI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQ---DASENELASFRQKEKELIDELRMATNENVD 368
Cdd:cd09236  94 LEEAMDILDDEASEDESLRRKFGTDRWTRPDSHEANPKLYTQAAEYEgylKQAGASDELVRRKLDEWEDLIQILTGDERD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 369 LEELLKGVTNGKAGLQFENNC--LVGKLEELSFVSD---------RNKQDADNARAQLEEE-----REKHRLATEKLHQE 432
Cdd:cd09236 174 LENFVPSSRRPSIPPELERHVraLRVSLEELDRLESrrrrkveraRTKARADDIRPEILREaarleREYPATEVAPAHFE 253
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 433 NI--DYMKTSDSRIEMILEESKTRkmmdESTIERLRldLDNEKSYKKNLEDLLNDLNQRALNS-EMANHLQKEGIQSVE 508
Cdd:cd09236 254 DLfdKRLAKYDKDLDAVSEEAQEQ----EEILQQIE--VANKAFLQSRKGDPATKERERALQSlDLAYFKYKEIVSNLD 326
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
217-426 7.95e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 7.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 217 TAKKKLVDMEHMVDELESENRNLTEKgrelkliIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESR 296
Cdd:COG3883  13 FADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 297 AALRDEQRHLEHQEAENGKI---------------VEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRM 361
Cdd:COG3883  86 EELGERARALYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 362 ATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-540 8.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVtNKRDTAKS---------SQQREQELSNILEE 280
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKGkcpvcgrelTEEHRKELLEEYTA 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  281 KEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNE-KLTMQVKDLQDASEN--ELASFRQKEKELID 357
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKaeEYEKLKEKLIKLKG 539
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  358 ELRMATNENVDLEEL---LKGVTNGKAGLQFENNCLVGKLEELSFVSdrnkqdadnaraqlEEEREKHRLATEKLHQENI 434
Cdd:PRK03918 540 EIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELEELGFES--------------VEELEERLKELEPFYNEYL 605
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660  435 DyMKTSDSRIEMILEESKTrkmmDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANhlQKEGIQSVETYLQMA 514
Cdd:PRK03918 606 E-LKDAEKELEREEKELKK----LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGL 678
                        330       340
                 ....*....|....*....|....*.
gi 17539660  515 KKRIEHLELELSATNATIEFQSQQLD 540
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELE 704
 
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