NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4506967|ref|NP_003027|]
View 

ski oncogene [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 91-192 9.64e-62

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


:

Pssm-ID: 410786  Cd Length: 102  Bit Score: 201.84  E-value: 9.64e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083   1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                        90       100
                ....*....|....*....|..
gi 4506967  171 APSCGLITKTDAERLCNALLYG 192
Cdd:cd21083  81 APSCGLITKTDAERLCNALLYG 102
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 217-311 2.49e-52

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4


:

Pssm-ID: 462602  Cd Length: 94  Bit Score: 175.92  E-value: 2.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 4506967    297 QARLGRCLDDVKEKF 311
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-709 1.67e-10

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 615
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     616 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 695
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 4506967     696 EHLEKVVKELQEQL 709
Cdd:TIGR02168  368 EELESRLEELEEQL 381
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.67e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 4506967   466 ETLAP-----VAAPEEDK 478
Cdd:PTZ00449 740 DAEQPddiefFTPPEEER 757
 
Name Accession Description Interval E-value
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 91-192 9.64e-62

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410786  Cd Length: 102  Bit Score: 201.84  E-value: 9.64e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083   1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                        90       100
                ....*....|....*....|..
gi 4506967  171 APSCGLITKTDAERLCNALLYG 192
Cdd:cd21083  81 APSCGLITKTDAERLCNALLYG 102
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 217-311 2.49e-52

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4


Pssm-ID: 462602  Cd Length: 94  Bit Score: 175.92  E-value: 2.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 4506967    297 QARLGRCLDDVKEKF 311
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 92-190 4.43e-52

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 175.54  E-value: 4.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     92 MPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSA 171
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90
                  ....*....|....*....
gi 4506967    172 PSCGLITKTDAERLCNALL 190
Cdd:pfam02437  81 RRCGLITKTDAERLCDALL 99
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 217-312 6.49e-52

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.


Pssm-ID: 198114  Cd Length: 95  Bit Score: 174.86  E-value: 6.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYtGKEE 296
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 4506967     297 QARLGRCLDDVKEKFD 312
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-709 1.67e-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: 64.69  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 615
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     616 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 695
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 4506967     696 EHLEKVVKELQEQL 709
Cdd:TIGR02168  368 EELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-727 3.32e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 616
Cdd:COG1196 218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  617 ERLRAE---NEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRERE 693
Cdd:COG1196 298 ARLEQDiarLEERRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                       170       180       190
                ....*....|....*....|....*....|....
gi 4506967  694 AREHLEKVVKELQEQlwpRARPEAAGSEGAAELE 727
Cdd:COG1196 373 ELAEAEEELEELAEE---LLEALRAAAELAAQLE 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
539-707 5.13e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   539 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 617
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   618 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 4506967   695 REHLEKVVKELQE 707
Cdd:PRK03918 710 KKELEKLEKALER 722
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 556-709 4.26e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    556 KEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRL 635
Cdd:pfam13868  47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506967    636 RLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHlEKVVKELQEQL 709
Cdd:pfam13868 127 QLREEIDEFNEEQ------AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRAQQ 193
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.67e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 4506967   466 ETLAP-----VAAPEEDK 478
Cdd:PTZ00449 740 DAEQPddiefFTPPEEER 757
growth_prot_Scy NF041483
polarized growth protein Scy;
603-727 1.85e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.74  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    603 REATEAKRNLRKEIERLRAENEKKMK----EANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAE 678
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQAEevraAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 4506967    679 ADREQLRadllreREAREHLEKV-------VKELQ---EQLWPRARPEAAGSEGAAELE 727
Cdd:NF041483  600 AEAERIR------REAAEETERLrteaaerIRTLQaqaEQEAERLRTEAAADASAARAE 652
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 543-605 1.87e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 40.37  E-value: 1.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506967  543 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 605
Cdd:cd07613 157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQatqiLQQVTVKLEDRIREA 223
 
Name Accession Description Interval E-value
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 91-192 9.64e-62

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410786  Cd Length: 102  Bit Score: 201.84  E-value: 9.64e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083   1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                        90       100
                ....*....|....*....|..
gi 4506967  171 APSCGLITKTDAERLCNALLYG 192
Cdd:cd21083  81 APSCGLITKTDAERLCNALLYG 102
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 93-191 2.43e-58

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410787  Cd Length: 100  Bit Score: 192.48  E-value: 2.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   93 PSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAP 172
Cdd:cd21084   1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                        90
                ....*....|....*....
gi 4506967  173 SCGLITKTDAERLCNALLY 191
Cdd:cd21084  81 SCGLITLTDAQRLCNALLR 99
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 100-190 9.04e-58

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410782  Cd Length: 91  Bit Score: 190.47  E-value: 9.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  100 RCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITK 179
Cdd:cd21079   1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                        90
                ....*....|.
gi 4506967  180 TDAERLCNALL 190
Cdd:cd21079  81 TDAERLCSALL 91
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 217-311 2.49e-52

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4


Pssm-ID: 462602  Cd Length: 94  Bit Score: 175.92  E-value: 2.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 4506967    297 QARLGRCLDDVKEKF 311
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 92-190 4.43e-52

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 175.54  E-value: 4.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     92 MPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSA 171
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90
                  ....*....|....*....
gi 4506967    172 PSCGLITKTDAERLCNALL 190
Cdd:pfam02437  81 RRCGLITKTDAERLCDALL 99
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 217-312 6.49e-52

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.


Pssm-ID: 198114  Cd Length: 95  Bit Score: 174.86  E-value: 6.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYtGKEE 296
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 4506967     297 QARLGRCLDDVKEKFD 312
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 103-187 1.14e-33

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. Members of this family include the Ski protein, Ski-like protein (Sno), and Dachshund proteins. Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development.


Pssm-ID: 410781  Cd Length: 88  Bit Score: 123.94  E-value: 1.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  103 TVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDA 182
Cdd:cd21074   4 STLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISKSDA 83


                ....*
gi 4506967  183 ERLCN 187
Cdd:cd21074  84 ERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 104-190 9.97e-20

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and similar proteins; Skor1, also known as functional Smad-suppressing element on chromosome 15 (Fussel-15), LBX1 corepressor 1, or ladybird homeobox corepressor 1, acts as a transcriptional corepressor of LBX1 and inhibits BMP signaling. Skor2, also known as functional Smad-suppressing element on chromosome 18 (Fussel-18), LBX1 corepressor 1-like protein, or ladybird homeobox corepressor 1-like protein, exhibits transcriptional repressor activity. It acts as a transforming growth factor-beta (TGF-beta) antagonist in the nervous system. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410783  Cd Length: 91  Bit Score: 84.42  E-value: 9.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  104 VLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAE 183
Cdd:cd21080   5 ILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAE 84


                ....*..
gi 4506967  184 RLCNALL 190
Cdd:cd21080  85 RLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-709 1.67e-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: 64.69  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 615
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     616 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 695
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 4506967     696 EHLEKVVKELQEQL 709
Cdd:TIGR02168  368 EELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-727 3.32e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 616
Cdd:COG1196 218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  617 ERLRAE---NEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRERE 693
Cdd:COG1196 298 ARLEQDiarLEERRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                       170       180       190
                ....*....|....*....|....*....|....
gi 4506967  694 AREHLEKVVKELQEQlwpRARPEAAGSEGAAELE 727
Cdd:COG1196 373 ELAEAEEELEELAEE---LLEALRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-709 2.04e-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: 57.76  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKL-----------------SAALQAKRSLHQELEFLRVAKKE 600
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeleekleelkeeleslEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     601 KLREATEAKRNLRKEIERLRAE---NEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHA 677
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190
                   ....*....|....*....|....*....|..
gi 4506967     678 EADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
541-710 6.22e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 6.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  541 ELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL-----RVAKKEKLREATEAKRNLRKE 615
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEER 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  616 IERLRaENEKKMKEANESRLRLKRELEQARQarvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 695
Cdd:COG4717 155 LEELR-ELEEELEELEAELAELQEELEELLE-----------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                       170
                ....*....|....*
gi 4506967  696 EHLEKVVKELQEQLW 710
Cdd:COG4717 223 EELEEELEQLENELE 237
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 103-187 1.34e-07

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar proteins; SKIDA1 is also known as protein DLN-1. Its biological function remains unclear. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410785  Cd Length: 91  Bit Score: 49.65  E-value: 1.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  103 TVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDA 182
Cdd:cd21082   4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDV 83


                ....*
gi 4506967  183 ERLCN 187
Cdd:cd21082  84 ERLYS 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 573-709 2.45e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     573 QEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKkmkeANESRLRLKRELEQARQARvcdk 652
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEI---- 763

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4506967     653 gceagrlrAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:TIGR02168  764 --------EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
539-707 5.13e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   539 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 617
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   618 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 4506967   695 REHLEKVVKELQE 707
Cdd:PRK03918 710 KKELEKLEKALER 722
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-709 5.24e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 5.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL---RVAKKEKLREATEAKRNLRK 614
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     615 EIERLRAENEKKMKEANESRLRLKRELEQARQARvcDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                          170
                   ....*....|....*
gi 4506967     695 REHLEKVVKELQEQL 709
Cdd:TIGR02168  861 IEELEELIEELESEL 875
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 572-709 6.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 6.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  572 KQEEKLSA-ALQAKR--SLHQELEFLRV-AKKEKLREATEAKRNLRKEIERLRAENEKKMK-----EANESRLRLKRELE 642
Cdd:COG1196 200 RQLEPLERqAEKAERyrELKEELKELEAeLLLLKLRELEAELEELEAELEELEAELEELEAelaelEAELEELRLELEEL 279

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506967  643 QARQArvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:COG1196 280 ELELE-------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 538-727 7.27e-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: 52.07  E-value: 7.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIE 617
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAELEKEIAELRAELE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEKKMKEA--------------------NESRLRLKRELEQARQARVcdkgceagrlrAKYSAQIEDLQVKLQHA 677
Cdd:COG4942 101 AQKEELAELLRALyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQA-----------EELRADLAELAALRAEL 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4506967  678 EADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
537-727 8.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   537 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 616
Cdd:COG4913  239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   617 ERLRAE---NEKKMKEANESRL-RLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKlqhAEADREQLRADLLRER 692
Cdd:COG4913  319 DALREEldeLEAQIRGNGGDRLeQLEREIERLERELE-----ERERRRARLEALLAALGLP---LPASAEEFAALRAEAA 390

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4506967   693 EAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:COG4913  391 ALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-728 1.46e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLHEVvKMRVKQeekLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 617
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDEL-RAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     618 RLRAENEKKMKEANESRLRLKRELEQARQARVCDKgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 697
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALA--LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170       180       190
                   ....*....|....*....|....*....|.
gi 4506967     698 LEKVVKELQEQLWPRARPEAagsEGAAELEP 728
Cdd:TIGR02168  934 LEVRIDNLQERLSEEYSLTL---EEAEALEN 961
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 576-709 1.58e-06

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: 49.92  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  576 KLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcdkgce 655
Cdd:COG1579  18 ELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK------- 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506967  656 agrlrakysaQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:COG1579  90 ----------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
547-709 1.61e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  547 QALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKK--EKLREATEAKRNLRKEIERLRA--E 622
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEEleE 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  623 NEKKMKEANESRLRLKRELEQARQARVcdkgceagRLRAKYSAQIEDlqvKLQHAEADREQLRADLLREREAREHLEKVV 702
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELE--------ELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEEL 222


                ....*..
gi 4506967  703 KELQEQL 709
Cdd:COG4717 223 EELEEEL 229
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
570-727 2.85e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.26  E-value: 2.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  570 RVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAkrNLRKEIERLRAENEKKMKEANESRLR-LKRELEQARQAR 648
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA--EERREAETARAEAEAAYEIAEANAEReVQRQLEIAERER 290

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506967  649 vcdkgceagrlrakysaqiedlQVKLQHAEADREQLRADllREREAREHLEKVVKELQEqlwpRARPEAAGSEGAAELE 727
Cdd:COG2268 291 ----------------------EIELQEKEAEREEAELE--ADVRKPAEAEKQAAEAEA----EAEAEAIRAKGLAEAE 341
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
538-709 2.88e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   538 LEAELEHLRQALEGGLDTKEAKEKF--LHEVVKMRVKQEEKLSAAL--QAKRSLHQELEFLRVAKKE---KLREATEAKR 610
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERheLYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEieeEISKITARIG 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   611 NLRKEIERLRaENEKKMKEANESRLRLKRELEQArqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR 690
Cdd:PRK03918 416 ELKKEIKELK-KAIEELKKAKGKCPVCGRELTEE----------HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484

                        170       180
                 ....*....|....*....|.
gi 4506967   691 EREAREHLEKVVK--ELQEQL 709
Cdd:PRK03918 485 LEKVLKKESELIKlkELAEQL 505
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
538-709 4.47e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 4.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSaalQAKRSLHQELEFLRVAKkEKLREATEAKRNLRKEIE 617
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE---ELNEQLQAAQAELAQAQ-EELESLQEEAEELQEELE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEKKMKEANESRLRLKrELEQARQARvcdkgceagrlrakySAQIEDLQVKLQHAEADREQLRADL--LREREAR 695
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIA-ELQSEIAER---------------EEELKELEEQLESLQEELAALEQELqaLSEAEAE 182

                       170
                ....*....|....
gi 4506967  696 EHLEKVVKELQEQL 709
Cdd:COG4372 183 QALDELLKEANRNA 196
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
556-707 4.48e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.86  E-value: 4.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  556 KEAKEKFLHEVVKMRVKQEEKLSAALQAKR-----SLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAEN---EKKM 627
Cdd:COG2433 357 KKVPPDVDRDEVKARVIRGLSIEEALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeelEAEL 436

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  628 KEANESRLRLKRELEQARQARvcdkgceagRLRAKYSAQIEDLQVKLqhaeadrEQLRADLLREREAREHLEKVVKELQE 707
Cdd:COG2433 437 EEKDERIERLERELSEARSEE---------RREIRKDREISRLDREI-------ERLERELEEERERIEELKRKLERLKE 500
PTZ00121 PTZ00121
MAEBL; Provisional
 473-703 4.80e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    473 APEEDKDSEAEVEVESREEFTSSLSSLSSPSFTSSSSAKDLGSPGARALPSAVPDAAAPADAPSGLEAELEHLRQALEGG 552
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    553 LDTKEAKEKflHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAK--KEKLREATEAKRNLRKEIERLRAENEKKMKEA 630
Cdd:PTZ00121 1391 KKADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506967    631 NESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVK 703
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
PTZ00121 PTZ00121
MAEBL; Provisional
 538-721 5.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    538 LEAELEHLRQALEGGLDTKEAKEKflheVVKMRVKQEEKLSAALQAKRSLHQELEFLRVA----KKEKLREATEAKR--- 610
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKKade 1550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    611 -----NLRKEIERLRAENEKKMKEANESRLRLKRELEQARQAR---VCDKGCEAGRLRAKYSAQIEDLQVK---LQHAEA 679
Cdd:PTZ00121 1551 lkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieeVMKLYEEEKKMKAEEAKKAEEAKIKaeeLKKAEE 1630

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 4506967    680 DREQLRADLLREREAREHLEKVVKElQEQLWPRARPEAAGSE 721
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAE 1671
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
540-709 1.53e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   540 AELEHLRQALEGGLDTKEAKekflHEVVKMRVKQEEKLSAaLQAKRSLHQELeflRVAKKEKLREATEAKRNLRKEIERL 619
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEER----LERAEDLVEAEDRIER-LEERREDLEEL---IAERRETIEEKRERAEELRERAAEL 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   620 RAENEKKMKEANESRlrlkrelEQARQARVCDKGCEagRLRAKYSAQIEDLQvKLQHAEADREQLRADLLREREAREHLE 699
Cdd:PRK02224 550 EAEAEEKREAAAEAE-------EEAEEAREEVAELN--SKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALA 619

                        170
                 ....*....|
gi 4506967   700 KVVKELQEQL 709
Cdd:PRK02224 620 ELNDERRERL 629
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
542-727 2.21e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  542 LEHLRQALEGGLDtKEAKEKF-----LHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 616
Cdd:COG4717  40 LAFIRAMLLERLE-KEADELFkpqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  617 ERLR-----AENEKKMKEANESRLRLKRELEQARQARvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADLLRE 691
Cdd:COG4717 119 EKLEkllqlLPLYQELEALEAELAELPERLEELEERL----------------EELRELEEELEELEAELAELQEELEEL 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4506967  692 RE-----AREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:COG4717 183 LEqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-698 2.37e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEgglDTKEAKEKFLHEVVKMRVkQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 617
Cdd:TIGR02168  836 TERRLEDLEEQIE---ELSEDIESLAAEIEELEE-LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     618 RLRAENEKKMKEANESRLRLKR-ELEQARQarvcdkgceAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 696
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGlEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 4506967     697 HL 698
Cdd:TIGR02168  983 EL 984
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 538-709 3.85e-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: 45.69  E-value: 3.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLR---- 613
Cdd:COG1579  15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKeyea 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  614 --KEIERLRAEN---EKKMKEANESRLRLKRELEQARqarvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADL 688
Cdd:COG1579  94 lqKEIESLKRRIsdlEDEILELMERIEELEEELAELE-------------------AELAELEAELEEKKAELDEELAEL 154

                       170       180
                ....*....|....*....|..
gi 4506967  689 LREREA-REHLEKVVKELQEQL 709
Cdd:COG1579 155 EAELEElEAEREELAAKIPPEL 176
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 556-709 4.26e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    556 KEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRL 635
Cdd:pfam13868  47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506967    636 RLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHlEKVVKELQEQL 709
Cdd:pfam13868 127 QLREEIDEFNEEQ------AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRAQQ 193
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 537-707 4.89e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     537 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAK-RSLHQELEFLRVAKKEKLREATEAKRNLRK- 614
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKl 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     615 --EIERLRAENEKkmkeanesrlrLKRELEQaRQARVCDKGCEAGRLRAKYsaqiEDLQVKLQHAEADREQLRADLlreR 692
Cdd:TIGR02169  328 eaEIDKLLAEIEE-----------LEREIEE-ERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDEL---K 388

                          170
                   ....*....|....*
gi 4506967     693 EAREHLEKVVKELQE 707
Cdd:TIGR02169  389 DYREKLEKLKREINE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-709 4.97e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   538 LEAELEHLRQALEGgLDTKEA---KEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEkLREATEAKRNLRK 614
Cdd:COG4913  622 LEEELAEAEERLEA-LEAELDalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD-LAALEEQLEELEA 699

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   615 EIERLRAEnekkMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:COG4913  700 ELEELEEE----LDELKGEIGRLEKELEQAEE-------------------ELDELQDRLEAAEDLARLELRALLEERFA 756

                        170
                 ....*....|....*
gi 4506967   695 REHLEKVVKELQEQL 709
Cdd:COG4913  757 AALGDAVERELRENL 771
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
572-709 5.91e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 5.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  572 KQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAEnekkMKEANESRLRLKRELEQARQArvcd 651
Cdd:COG4372   3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREE----LEQAREELEQLEEELEQARSE---- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506967  652 kgceagrlRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:COG4372  75 --------LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
PRK12704 PRK12704
phosphodiesterase; Provisional
 569-708 6.43e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   569 MRVKQEEKLSAA-LQAKRSLHQELEFLRVAKKEKLREATEakrnlrkEIERLRAENEKKMKEAN------ESRLRLKREL 641
Cdd:PRK12704  25 RKKIAEAKIKEAeEEAKRILEEAKKEAEAIKKEALLEAKE-------EIHKLRNEFEKELRERRnelqklEKRLLQKEEN 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506967   642 EQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR-----EREAREH-LEKVVKELQEQ 708
Cdd:PRK12704  98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEIlLEKVEEEARHE 170
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
574-714 6.79e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 6.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  574 EEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcdkg 653
Cdd:COG4372  30 SEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----- 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506967  654 ceagrlrakysAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRAR 714
Cdd:COG4372 101 -----------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
540-709 1.50e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   540 AELEHLRQALEGGLDTKEAKEKFLHEVVKmRVKQeeklsaaLQAKRSLHQELEFLRVAKKEKLREATEAK---RNLRKEI 616
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVK-ELKE-------LKEKAEEYIKLSEFYEEYLDELREIEKRLsrlEEEINGI 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   617 ERLRAENEKKMKEANESRLRLK-------------RELEQARQarvcdKGCEAGRLRAKYSA-QIEDLQVKLQHAEADRE 682
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKelekrleeleerhELYEEAKA-----KKEELERLKKRLTGlTPEKLEKELEELEKAKE 401

                        170       180
                 ....*....|....*....|....*..
gi 4506967   683 QLRADLLREREAREHLEKVVKELQEQL 709
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAI 428
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 610-708 1.82e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 43.36  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    610 RNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRA 686
Cdd:pfam13851  29 KSLKEEIAELKkkeERNEKLMSEIQQENKRLTEPLQKAQE-------------------EVEELRKQLENYEKDKQSLKN 89

                          90       100
                  ....*....|....*....|..
gi 4506967    687 dlLREReaREHLEKVVKELQEQ 708
Cdd:pfam13851  90 --LKAR--LKVLEKELKDLKWE 107
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-726 2.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIE 617
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEA 452

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEkkmkEANESRLRLKRELEQARQArvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 697
Cdd:COG1196 453 ELEEEEE----ALLELLAELLEEAALLEAA----------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                       170       180
                ....*....|....*....|....*....
gi 4506967  698 LEKVVKELQEQLWPRARPEAAGSEGAAEL 726
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAA 547
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 538-716 2.60e-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: 44.58  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEK-LSAALQAKRSLHQELEFLRVAKKEKLREATEAKRN---LR 613
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKeNKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvdDE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     614 KEIERLRAENEKKMKEAN---ESRLRLKRELEqarqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR 690
Cdd:pfam02463  314 EKLKESEKEKKKAEKELKkekEEIEELEKELK------------ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381

                          170       180
                   ....*....|....*....|....*.
gi 4506967     691 EreaREHLEKVVKELQEQLWPRARPE 716
Cdd:pfam02463  382 E---SERLSSAAKLKEEELELKSEEE 404
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 540-709 2.85e-04

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 42.59  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    540 AELEHLRQALEGGLdtkEAKEKFLHEVVKMRVKQeeklsAALQAKRSLHQE----LEFLRVAkkEKLREATEAKRNLRKE 615
Cdd:pfam09727   5 DDLLKLLSILEGEL---QARDIVIAVLKAEKVKQ-----LLLEARYGFKYPsdplLALQRDS--ELLRDQSQDEDVYEAM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    616 IERLRAENEKKMKEANESRLRLKRELEQA--RQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHaeaDREQLRADLLRERE 693
Cdd:pfam09727  75 YEKPLAELEKLVEKQRETQRRMLEQLAAAekRHRRVIRELEEEKRKHARDTAQGDDFTYLLEK---ERERLKQELEQEKA 151

                         170
                  ....*....|....*.
gi 4506967    694 AREHLEKVVKELQEQL 709
Cdd:pfam09727 152 QQKRLEKELKKLLEKL 167
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
556-707 2.91e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   556 KEAKEKF---LHEVVKMRvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLR------KEIERLRAENEKK 626
Cdd:PRK03918 196 KEKEKELeevLREINEIS-SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   627 MKEANESRLRLK---------RELEQARQARVcDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR-- 695
Cdd:PRK03918 275 IEELEEKVKELKelkekaeeyIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkr 353

                        170
                 ....*....|...
gi 4506967   696 -EHLEKVVKELQE 707
Cdd:PRK03918 354 lEELEERHELYEE 366
PTZ00121 PTZ00121
MAEBL; Provisional
 541-708 2.97e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    541 ELEHLRQALEGGLDTKEAKEKFLHEVvkMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRN-----LRKE 615
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeaeeKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    616 IERLRAENEKKMKEANESRL--RLKRELEQARQARVCD-KGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADllrER 692
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEkKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EE 1726

                         170
                  ....*....|....*.
gi 4506967    693 EAREHLEKVVKELQEQ 708
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEED 1742
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 538-707 3.40e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLhevVKMRVKQEEKLSAALQAKRSLHQELEFL--RVAKKEKLREATEAKRN-LRK 614
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALERQKEAIerQLASLEEELEKLTEEISeLEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     615 EIE----RLRAENEKKMKEANESRLRLKRELE--QARQARVCDKGCEAGR--------------LRAKYSAQIEDLQVKL 674
Cdd:TIGR02169  266 RLEeieqLLEELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIAEKEReledaeerlakleaEIDKLLAEIEELEREI 345

                          170       180       190
                   ....*....|....*....|....*....|...
gi 4506967     675 QHAEADREQLRADLlreREAREHLEKVVKELQE 707
Cdd:TIGR02169  346 EEERKRRDKLTEEY---AELKEELEDLRAELEE 375
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 539-708 3.54e-04

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: 43.94  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    539 EAELEHLRQALEggldtkeAKEKFLHEVvkmrvKQEEKLSAALQAKRslhQELEFLRVAKKEKLRE-------ATEAKRN 611
Cdd:pfam05483 404 EVELEELKKILA-------EDEKLLDEK-----KQFEKIAEELKGKE---QELIFLLQAREKEIHDleiqltaIKTSEEH 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    612 LRKEIERLRAENEK-KMKE----ANESRLRLK-RELEQarqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLR 685
Cdd:pfam05483 469 YLKEVEDLKTELEKeKLKNieltAHCDKLLLEnKELTQ-----------EASDMTLELKKHQEDIINCKKQEERMLKQIE 537

                         170       180
                  ....*....|....*....|...
gi 4506967    686 ADLLREREAREHLEKVVKELQEQ 708
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQK 560
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 589-722 3.57e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   589 QELEFLRVAKKEKLREATEakrnLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVcdkgCEAGRLRAKYSAQIE 668
Cdd:PRK00409 523 ASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI----KEAKKEADEIIKELR 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4506967   669 DLQvKLQHAEADREQLradllreREAREHLEKVVKELQEQLWPRARPEAAGSEG 722
Cdd:PRK00409 595 QLQ-KGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 572-704 3.70e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 40.63  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    572 KQEEKLSAALQAKRSLHQELEflrvakkeklREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcd 651
Cdd:pfam13863   6 REMFLVQLALDAKREEIERLE----------ELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEET--- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4506967    652 kgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKE 704
Cdd:pfam13863  73 ------KLKKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEKVVPK 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 538-709 3.83e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGgLDTKEAKEKFLHEVVKMRVKQ-EEKLSAALQAKRSLHQELEFLRvAKKEKLREATEA-------- 608
Cdd:TIGR02169  714 ASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSlEQEIENVKSELKELEARIEELE-EDLHKLEEALNDlearlshs 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     609 ----KRNLRKEIERLRAENEKKMKEAN--ESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADRE 682
Cdd:TIGR02169  792 ripeIQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                          170       180
                   ....*....|....*....|....*..
gi 4506967     683 QLRADLLREREAREHLEKVVKELQEQL 709
Cdd:TIGR02169  872 ELEAALRDLESRLGDLKKERDELEAQL 898
PTZ00121 PTZ00121
MAEBL; Provisional
 556-725 4.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    556 KEAKEKFLHEVVKmrvKQEEKLSAALQAKRSLHQEleflrVAKKEKLREATEAKRnLRKEIERLRAENEKK----MKEAN 631
Cdd:PTZ00121 1614 KAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEE-----KKKAEELKKAEEENK-IKAAEEAKKAEEDKKkaeeAKKAE 1684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    632 ESRLR----LKRELEQARQARVCDKGCEAGRLRA---KYSAQIEDLQVKLQHAEADREQLRADLLR----EREAREHLEK 700
Cdd:PTZ00121 1685 EDEKKaaeaLKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeeEKKKIAHLKK 1764

                         170       180
                  ....*....|....*....|....*
gi 4506967    701 VVKELQEQLwpRARPEAAGSEGAAE 725
Cdd:PTZ00121 1765 EEEKKAEEI--RKEKEAVIEEELDE 1787
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 101-185 5.63e-04

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 39.65  E-value: 5.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  101 CETV-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLI 177
Cdd:cd21081   3 CKMVeYRGAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLI 82


                ....*...
gi 4506967  178 TKTDAERL 185
Cdd:cd21081  83 SRKDFDTL 90
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 540-709 6.32e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    540 AELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAK----RSLHQELEFLRVAKKEK---LREATEAKRNL 612
Cdd:pfam05557  30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaelnRLKKKYLEALNKKLNEKesqLADAREVISCL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    613 RKEIERLRAENEKKMKEANESRLRLK--RELEQARQARVcdkgceagrlrAKYSAQIEDLQVKlQHAEADREQLRADLLR 690
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEelQERLDLLKAKA-----------SEAEQLRQNLEKQ-QSSLAEAEQRIKELEF 177

                         170
                  ....*....|....*....
gi 4506967    691 EREAREHLEKVVKELQEQL 709
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSEL 196
PRK11020 PRK11020
YibL family ribosome-associated protein;
569-647 6.82e-04

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 40.01  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   569 MRVKQE-EKLSAALQAKRslHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKM-KEANE-SRLRLKRELEQAR 645
Cdd:PRK11020   1 MVEKNEiKRLSDRLDAIR--HKLAAASLRGDAEKYAQFEKEKATLEAEIARLKEVQSQKLsKEAQKlMKLPFSRAITKKE 78


                 ..
gi 4506967   646 QA 647
Cdd:PRK11020  79 QA 80
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 555-709 7.12e-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: 7.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     555 TKEAK--EKFLHEVVKMRVKQEEKlSAALQAKRSLHQ----ELEfLRVAKKEKLREATE-AKRNLRKEIERLRAENEKKM 627
Cdd:pfam01576  151 SKERKllEERISEFTSNLAEEEEK-AKSLSKLKNKHEamisDLE-ERLKKEEKGRQELEkAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     628 KEANESRLRL-KRELE-QARQARVCDKGceagrlrakysAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKEL 705
Cdd:pfam01576  229 AQIAELRAQLaKKEEElQAALARLEEET-----------AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297


                   ....
gi 4506967     706 QEQL 709
Cdd:pfam01576  298 GEEL 301
PTZ00121 PTZ00121
MAEBL; Provisional
 543-700 7.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    543 EHLRQALEGGLDTKEAKEKFLHEVVK---MRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERL 619
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    620 RAENEKKMKEANESRLRLKRELEQARQARV--CDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA--R 695
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviE 1782


                  ....*
gi 4506967    696 EHLEK 700
Cdd:PTZ00121 1783 EELDE 1787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
538-709 9.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   538 LEAELEHLRQALEGGldTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNL-RKEI 616
Cdd:COG4913  267 ARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDELEAQIRGNgGDRL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   617 ERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAG---------RLRAKYSAQIEDLQVKLQHAEADREQLRAD 687
Cdd:COG4913  341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalraeaaALLEALEEELEALEEALAEAEAALRDLRRE 420

                        170       180       190
                 ....*....|....*....|....*....|...
gi 4506967   688 L------LREREAR-----EHLEKVVKELQEQL 709
Cdd:COG4913  421 LreleaeIASLERRksnipARLLALRDALAEAL 453
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 576-727 1.01e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     576 KLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANesRLRLKRELEQARQARVCDKGCE 655
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506967     656 AGRLRAKYSAQIEDLQVKLQHAEADREQLRADL--LREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 538-709 1.09e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 40.71  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    538 LEAELEHLRQALEGGL-DTKEAKEKFLHEVVKMrvkqeeklsaalqakrsLHQELEFLRvakkEKLREATEAKRN-LRKE 615
Cdd:pfam01442  31 LEKETEALRERLQKDLeEVRAKLEPYLEELQAK-----------------LGQNVEELR----QRLEPYTEELRKrLNAD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    616 IERLRAENEKKMKEANEsrlRLKRELEQARqARVcdkGCEAGRLRAKYSAQIEDLQVKLQ-HAEADREQLRadlLREREA 694
Cdd:pfam01442  90 AEELQEKLAPYGEELRE---RLEQNVDALR-ARL---APYAEELRQKLAERLEELKESLApYAEEVQAQLS---QRLQEL 159

                         170
                  ....*....|....*
gi 4506967    695 REHLEKVVKELQEQL 709
Cdd:pfam01442 160 REKLEPQAEDLREKL 174
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 543-721 1.28e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    543 EHLRQALEGG----LDTKEAKEKFLHEVVKM---RVKQEEKLSAALQA---------KRSLHQELEflRVAKKEKLREAT 606
Cdd:pfam17380 392 ERVRQELEAArkvkILEEERQRKIQQQKVEMeqiRAEQEEARQREVRRleeeraremERVRLEEQE--RQQQVERLRQQE 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    607 EAKRNLRKEIERlraENEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADR---EQ 683
Cdd:pfam17380 470 EERKRKKLELEK---EKRDRKRAEEQRRKILEKELEERKQAMI-----EEERKRKLLEKEMEERQKAIYEEERRReaeEE 541

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 4506967    684 LRADllREREAREHLEKVVKELQEQlwpRARPEAAGSE 721
Cdd:pfam17380 542 RRKQ--QEMEERRRIQEQMRKATEE---RSRLEAMERE 574
Filament pfam00038
Intermediate filament protein;
570-709 1.29e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    570 RVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATeaKRNLRKEIERLRAEnekkmkeanesRLRLKRELEQARQArv 649
Cdd:pfam00038  19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKE--IEDLRRQLDTLTVE-----------RARLQLELDNLRLA-- 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    650 cdkgceAGRLRAKYsaqiEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:pfam00038  84 ------AEDFRQKY----EDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEEL 133
mukB PRK04863
chromosome partition protein MukB;
556-718 1.41e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    556 KEAKEKFLHEVVKMRVKQE--EKLSAALQAKRSLHQELEflRVAKKEKLREATEAKRNLRKEIERLRAEnEKKMKEAnES 633
Cdd:PRK04863  452 QEATEELLSLEQKLSVAQAahSQFEQAYQLVRKIAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQL-RMRLSEL-EQ 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    634 RLRLKRELEQA------RQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKvvkelQE 707
Cdd:PRK04863  528 RLRQQQRAERLlaefckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-----RA 602

                         170
                  ....*....|.
gi 4506967    708 QLWPRARPEAA 718
Cdd:PRK04863  603 PAWLAAQDALA 613
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 538-709 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAElEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLsaalQAKRSLHQEleflRVAKKE-KLREATEAKRNLRKei 616
Cdd:pfam01576  112 LDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL----SKERKLLEE----RISEFTsNLAEEEEKAKSLSK-- 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     617 erLRAENEKKMKEANEsrlRLKRElEQARQARVCDK---GCEAGRLR---AKYSAQIEDLQVKLQHAEADREQLRADLLR 690
Cdd:pfam01576  181 --LKNKHEAMISDLEE---RLKKE-EKGRQELEKAKrklEGESTDLQeqiAELQAQIAELRAQLAKKEEELQAALARLEE 254

                          170
                   ....*....|....*....
gi 4506967     691 EREAREHLEKVVKELQEQL 709
Cdd:pfam01576  255 ETAQKNNALKKIRELEAQI 273
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 538-724 1.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQ---ALEGGLDTKEAKEKFLHEVVKMRVKQEEK-------LSAALQAKrSLHqelEFL-RVAKKEKL---- 602
Cdd:COG3883  56 LQAELEALQAeidKLQAEIAEAEAEIEERREELGERARALYRsggsvsyLDVLLGSE-SFS---DFLdRLSALSKIadad 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  603 REATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADRE 682
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-----EQEALLAQLSAEEAAAEAQLAELEAELA 206

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4506967  683 QLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAA 724
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 596-713 1.57e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 39.94  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    596 VAKKEKLRE-----ATEAKRNLRKEIERLRAENEKKMKEANEsrlRLKRELEQARQARvcdkGCEAGRLRAKYSAQIEDL 670
Cdd:pfam01442  10 STYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRA---KLEPYLEELQAKL----GQNVEELRQRLEPYTEEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 4506967    671 QVKLqhaEADREQLRADLL-REREAREHLEKVVKELQEQLWPRA 713
Cdd:pfam01442  83 RKRL---NADAEELQEKLApYGEELRERLEQNVDALRARLAPYA 123
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 538-707 1.63e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.27  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    538 LEAELEHLRQaleggldTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLRKEIE 617
Cdd:pfam13851  31 LKEEIAELKK-------KEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYE-KDKQSLKNLKARLKVLEKELK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    618 RLRAENE-KKMKeanesrlrlKRELEQARQArvcdkgceagrLRAKYSAQIEDLQvklQHAEadreqLRADLLRER--EA 694
Cdd:pfam13851 103 DLKWEHEvLEQR---------FEKVERERDE-----------LYDKFEAAIQDVQ---QKTG-----LKNLLLEKKlqAL 154

                         170
                  ....*....|...
gi 4506967    695 REHLEKVVKELQE 707
Cdd:pfam13851 155 GETLEKKEAQLNE 167
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.67e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 4506967   466 ETLAP-----VAAPEEDK 478
Cdd:PTZ00449 740 DAEQPddiefFTPPEEER 757
PTZ00121 PTZ00121
MAEBL; Provisional
 539-707 1.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    539 EAELEHLRQALEGGLDTKEAKeKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvaKKEKLREATEakrnLRKEIER 618
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR--KADELKKAEE----KKKADEA 1295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    619 LRAENEKKMKEAnesrlrlKRELEQARQARVCDKGCEAGRLRA------------KYSAQIEDLQVKLQHAEADREQLRA 686
Cdd:PTZ00121 1296 KKAEEKKKADEA-------KKKAEEAKKADEAKKKAEEAKKKAdaakkkaeeakkAAEAAKAEAEAAADEAEAAEEKAEA 1368

                         170       180
                  ....*....|....*....|.
gi 4506967    687 DLLREREAREHLEKVVKELQE 707
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEE 1389
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
602-727 1.75e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  602 LREATEAKRNLRKEIERLRAENEKKMKEAN----ESRLRLKRELEQARQARvcdKGCEAGRLRAKY-----SAQIE-DLQ 671
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANreaeEAELEQEREIETARIAE---AEAELAKKKAEErreaeTARAEaEAA 267

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506967  672 VKLQHAEADREQLRADLLRERE-----AREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREreielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 568-709 1.82e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     568 KMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLR----KEIERLRAENEKKMKE--ANESRLRLKREL 641
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELEEEYLLYLDYlkLNEERIDLLQEL 245

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506967     642 EQARQAR----------VCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:pfam02463  246 LRDEQEEiesskqeiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
growth_prot_Scy NF041483
polarized growth protein Scy;
603-727 1.85e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.74  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    603 REATEAKRNLRKEIERLRAENEKKMK----EANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAE 678
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQAEevraAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 4506967    679 ADREQLRadllreREAREHLEKV-------VKELQ---EQLWPRARPEAAGSEGAAELE 727
Cdd:NF041483  600 AEAERIR------REAAEETERLrteaaerIRTLQaqaEQEAERLRTEAAADASAARAE 652
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 543-605 1.87e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 40.37  E-value: 1.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506967  543 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 605
Cdd:cd07613 157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQatqiLQQVTVKLEDRIREA 223
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 375-483 1.87e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   375 RLSAFRPWSPAVSASEKELSPHLPAlirdsfysyksfeTAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRK 454
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARP-------------EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV 426

                         90       100
                 ....*....|....*....|....*....
gi 4506967   455 RKLTVDTPGAPETLAPVAAPEEDKDSEAE 483
Cdd:PRK14951 427 AAPAAAAPAAAPAAAPAAVALAPAPPAQA 455
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 570-727 1.88e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    570 RVKQEEKLSAALQAKRSLHQ-ELEFLRvAKKEKLREATEAKRNLRKEIERLRAEnekkmkeanESRLRLKRELEQARQAr 648
Cdd:pfam05557   1 RAELIESKARLSQLQNEKKQmELEHKR-ARIELEKKASALKRQLDRESDRNQEL---------QKRIRLLEKREAEAEE- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506967    649 vcdkgceagrlraKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 727
Cdd:pfam05557  70 -------------ALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
538-719 1.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAAL----------QAKRSLHQELEFLRVAKKEKLREATE 607
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglddadaEAVEARREELEDRDEELRDRLEECRV 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   608 AKRNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQArVCDKGCEAGRLRAKY---SAQIEDLQVKLQHAEADR 681
Cdd:PRK02224 336 AAQAHNEEAESLRedaDDLEERAEELREEAAELESELEEAREA-VEDRREEIEELEEEIeelRERFGDAPVDLGNAEDFL 414

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4506967   682 EQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAG 719
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAG 452
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 574-676 2.24e-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: 41.31  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     574 EEKLSAALQAKRSLH---QELEFLRVAKKEKLREATEAKRNLRKEIERLRA---ENEKKMKE-------ANESRLRLKRE 640
Cdd:pfam01576  474 QELLQEETRQKLNLStrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlsDMKKKLEEdagtleaLEEGKKRLQRE 553

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 4506967     641 LEQARQaRVCDKGCEAGRL---RAKYSAQIEDLQVKLQH 676
Cdd:pfam01576  554 LEALTQ-QLEEKAAAYDKLektKNRLQQELDDLLVDLDH 591
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 538-707 2.25e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLR---QALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELeflrvakKEKLREATEAKRNLRK 614
Cdd:TIGR02169  327 LEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET-------RDELKDYREKLEKLKR 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     615 EIERLRAENEKKMKEANesrlRLKRELEQARQARvcdKGCEAGrlRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:TIGR02169  400 EINELKRELDRLQEELQ----RLSEELADLNAAI---AGIEAK--INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          170
                   ....*....|....*..
gi 4506967     695 ----REHLEKVVKELQE 707
Cdd:TIGR02169  471 lydlKEEYDRVEKELSK 487
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 541-708 2.49e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    541 ELEHLRQALEGGLDTKEAKEKFLHEVVKMRvkqeeklsaALQAKRSLHQELEflrVAKKEKLREATEAKRNLRKEIE--- 617
Cdd:pfam05557  22 ELEHKRARIELEKKASALKRQLDRESDRNQ---------ELQKRIRLLEKRE---AEAEEALREQAELNRLKKKYLEaln 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    618 RLRAENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakySAQIEDLQVKLQHAEADREQLRADLLRER----- 692
Cdd:pfam05557  90 KKLNEKESQLADAREVISCLKNELSELRR-----------------QIQRAELELQSTNSELEELQERLDLLKAKaseae 152

                         170
                  ....*....|....*.
gi 4506967    693 EAREHLEKVVKELQEQ 708
Cdd:pfam05557 153 QLRQNLEKQQSSLAEA 168
PRK12472 PRK12472
hypothetical protein; Provisional
 573-694 2.52e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.01  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   573 QEEKLSAALQAKRslhqeleflrvAKKEKLREATEAKRNLRKeIERLRAENEKKMKEANESRLRLKRELEQARqarvcdk 652
Cdd:PRK12472 199 AEDAARAADEAKT-----------AAAAAAREAAPLKASLRK-LERAKARADAELKRADKALAAAKTDEAKAR------- 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 4506967   653 gceAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 694
Cdd:PRK12472 260 ---AEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEA 298
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 553-710 2.65e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 39.75  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    553 LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKR----SLHQELEFLRVAKKEKLREATEAKrNLRKEIERLRAENEKKMK 628
Cdd:pfam14988  28 VQECEEIERRRQELASRYTQQTAELQTQLLQKEkeqaSLKKELQALRPFAKLKESQEREIQ-DLEEEKEKVRAETAEKDR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    629 EANESRLRLKRELE-QARQARVCDKGcEAGRLRAKYSAQIEDLQVKLQHAEADR------EQLRADLL-------REREA 694
Cdd:pfam14988 107 EAHLQFLKEKALLEkQLQELRILELG-ERATRELKRKAQALKLAAKQALSEFCRsikrenRQLQKELLqliqetqALEAI 185

                         170
                  ....*....|....*.
gi 4506967    695 REHLEKVVKELQEQLW 710
Cdd:pfam14988 186 KSKLENRKQRLKEEQW 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
544-708 2.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   544 HLRQA-LEGGLDTKEAKEKFLHEVVKMrvkqeEKLSAALQAKRSLHQELEFlRVAKKEKLREATEAKRNLRKEIERLRAE 622
Cdd:PRK03918 131 YIRQGeIDAILESDESREKVVRQILGL-----DDYENAYKNLGEVIKEIKR-RIERLEKFIKRTENIEELIKEKEKELEE 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   623 NEKKMKEANESRLRLKRELEQARQarvcdkgcEAGRLRaKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVV 702
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEK--------EVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275


                 ....*.
gi 4506967   703 KELQEQ 708
Cdd:PRK03918 276 EELEEK 281
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 593-709 3.05e-03

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: 41.09  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   593 FLRVA--KKEKLREATEAKRNLRKEIERLRAENE------KKMKEANESRLRLKRELEQARQ--ARVCdkgcEAGRLRAK 662
Cdd:COG3096  273 YMRHAneRRELSERALELRRELFGARRQLAEEQYrlvemaRELEELSARESDLEQDYQAASDhlNLVQ----TALRQQEK 348

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 4506967   663 ---YSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:COG3096  349 ierYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 540-728 3.08e-03

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: 40.65  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    540 AELEHLRQALEGGL-----DTKEAKEKFLHEVVKMRVKQEEkLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRK 614
Cdd:pfam07888  44 AELLQAQEAANRQRekekeRYKRDREQWERQRRELESRVAE-LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    615 EierlRAENEKKMKEANE--SRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRER 692
Cdd:pfam07888 123 Q----RAAHEARIRELEEdiKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 4506967    693 EAREHLEKVVKELQEQLWPRARPEAAGSEGAAELEP 728
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 538-709 3.23e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 3.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEA----KRNLR 613
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVELS-KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATledtLKAAD 419

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  614 KEIERLRAENEKKMKEaNESRLRLKRELEQARQARVCD-KGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLlreR 692
Cdd:COG5185 420 RQIEELQRQIEQATSS-NEEVSKLLNELISELNKVMREaDEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV---S 495

                       170
                ....*....|....*..
gi 4506967  693 EAREHLEKVVKELQEQL 709
Cdd:COG5185 496 TLKATLEKLRAKLERQL 512
PTZ00121 PTZ00121
MAEBL; Provisional
 574-708 3.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    574 EEKLSAALQAKRSlhqelEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANES----RLRLKRELEQARQARV 649
Cdd:PTZ00121 1094 EEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAedakRVEIARKAEDARKAEE 1168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 4506967    650 CDKGCEAGRLRAKYSAQIEDLQVKLQHAEADReqlRADLLREREAREHLEKVVKELQEQ 708
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDAR---KAEAARKAEEERKAEEARKAEDAK 1224
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
538-707 4.19e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKeakekflhevvkmrvkQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 617
Cdd:COG3206 238 AEARLAALRAQLGSGPDAL----------------PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEkkmKEANESRLRLKRELEQARQArvcdkgceagrlRAKYSAQIEDLQVKLQHAEADREQLRaDLLRERE-ARE 696
Cdd:COG3206 302 ALRAQLQ---QEAQRILASLEAELEALQAR------------EASLQAQLAQLEARLAELPELEAELR-RLEREVEvARE 365

                       170
                ....*....|.
gi 4506967  697 HLEKVVKELQE 707
Cdd:COG3206 366 LYESLLQRLEE 376
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 541-709 4.32e-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: 40.54  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     541 ELEHLRQALEGglDTKEAKEKF------LHEVVKMRVKQEEKLSAAL------QAKRSL----HQELEFLRVAKKEKLR- 603
Cdd:pfam01576  205 ELEKAKRKLEG--ESTDLQEQIaelqaqIAELRAQLAKKEEELQAALarleeeTAQKNNalkkIRELEAQISELQEDLEs 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     604 ------EATEAKRNLRKEIERLRAENEKKMKE-ANESRLRLKRELEQARQARVCD---KGCEA--GRLRAKYSAQIEDLQ 671
Cdd:pfam01576  283 eraarnKAEKQRRDLGEELEALKTELEDTLDTtAAQQELRSKREQEVTELKKALEeetRSHEAqlQEMRQKHTQALEELT 362

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 4506967     672 VKLQHAEADREQLradllreREAREHLEKVVKELQEQL 709
Cdd:pfam01576  363 EQLEQAKRNKANL-------EKAKQALESENAELQAEL 393
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 538-713 4.39e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.59  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKL--------------- 602
Cdd:pfam12128  324 LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiagikdklakir 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     603 ----REATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQAR--------------QARVCDKGCEAGR-LRAKY 663
Cdd:pfam12128  404 eardRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllQLENFDERIERAReEQEAA 483

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 4506967     664 SAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRA 713
Cdd:pfam12128  484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
PTZ00121 PTZ00121
MAEBL; Provisional
 555-718 4.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    555 TKEAKEKFlHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKR---NLRKEIERlRAENEKKMKEAN 631
Cdd:PTZ00121 1093 TEEAFGKA-EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKaedAKRVEIAR-KAEDARKAEEAR 1170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    632 ES----RLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADR--------EQLRADLLREREARE--H 697
Cdd:PTZ00121 1171 KAedakKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaeavkkaEEAKKDAEEAKKAEEerN 1250

                         170       180
                  ....*....|....*....|.
gi 4506967    698 LEKVVKELQEQLWPRARPEAA 718
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAA 1271
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 538-684 4.47e-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: 40.54  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     538 LEAELEHLRQALEGGLDT----KEAKEKFLHEVVKM-RVKQEEKLS--AALQAKRSLH-QELEFLrvakKEKLREATEAK 609
Cdd:pfam01576  297 LGEELEALKTELEDTLDTtaaqQELRSKREQEVTELkKALEEETRSheAQLQEMRQKHtQALEEL----TEQLEQAKRNK 372

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506967     610 RNLRKEIERLRAENEKKMKEAnesrlrlkRELEQARQarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQL 684
Cdd:pfam01576  373 ANLEKAKQALESENAELQAEL--------RTLQQAKQ--------DSEHKRKKLEGQLQELQARLSESERQRAEL 431
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
538-707 4.73e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   538 LEAELEHLRQA--LEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKE---KLREATEAKRNL 612
Cdd:PRK02224 494 VEERLERAEDLveAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREE 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   613 RKEIERLRAENEKKM---------------KEANESRLRLKR----ELEQARQARVCDKGCEAGRLRAKY-SAQIEDLQV 672
Cdd:PRK02224 574 VAELNSKLAELKERIeslerirtllaaiadAEDEIERLREKRealaELNDERRERLAEKRERKRELEAEFdEARIEEARE 653

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4506967   673 KLQHAEADREQLRADLLREREAREHLEK----VVKELQE 707
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLQAeigaVENELEE 692
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 538-709 5.72e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    538 LEAELEHLRQALEGG---LDTKEAKEKFLHEVVKmrvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRK 614
Cdd:TIGR04523 473 LSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKK---ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    615 EIERLRAENEKK-----------MKEANESRLRLKRELEQarqaRVCDKGCEAGRLR---AKYSAQIEDLQVKLQHAEAD 680
Cdd:TIGR04523 550 DDFELKKENLEKeideknkeieeLKQTQKSLKKKQEEKQE----LIDQKEKEKKDLIkeiEEKEKKISSLEKELEKAKKE 625

                         170       180
                  ....*....|....*....|....*....
gi 4506967    681 REQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 539-707 6.19e-03

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: 40.03  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     539 EAELEHLRQALEGgLDTKEAKEKflhevvkMRVKQEEKLSAALQAKRSLHQELEfLRVAKKEKLREATEakrNLRKEIER 618
Cdd:TIGR00606  743 EKEIPELRNKLQK-VNRDIQRLK-------NDIEEQETLLGTIMPEEESAKVCL-TDVTIMERFQMELK---DVERKIAQ 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967     619 LRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHL 698
Cdd:TIGR00606  811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890


                   ....*....
gi 4506967     699 EKVVKELQE 707
Cdd:TIGR00606  891 VELSTEVQS 899
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 537-707 6.22e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   537 GLEAELEHLRQALE------GGLDTKEAKEKfLHEVvkmrvkQEE--KLSAALQ----AKRSLHQELEFLrvakKEKLRE 604
Cdd:PRK04778 253 DIEKEIQDLKEQIDenlallEELDLDEAEEK-NEEI------QERidQLYDILErevkARKYVEKNSDTL----PDFLEH 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967   605 ATEAKRNLRKEIERLR-----AENEKkmkeanESRLRLKRELEQAR-QARVCDKGCEAGRLRakYS---AQIEDLQVKLQ 675
Cdd:PRK04778 322 AKEQNKELKEEIDRVKqsytlNESEL------ESVRQLEKQLESLEkQYDEITERIAEQEIA--YSelqEELEEILKQLE 393

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4506967   676 HAEADREQLRADL--LR--EREAREHLEKVVKELQE 707
Cdd:PRK04778 394 EIEKEQEKLSEMLqgLRkdELEAREKLERYRNKLHE 429
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 574-709 6.33e-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: 6.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  574 EEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKrelEQARQARVcdKG 653
Cdd:COG3883  29 QAELEAAQAELDALQAELE----ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ERARALYR--SG 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506967  654 CEAGRL--------------RAKYSAQIEDLQVK-LQHAEADREQLRADLLREREAREHLEKVVKELQEQL 709
Cdd:COG3883 100 GSVSYLdvllgsesfsdfldRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 556-701 6.38e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.28  E-value: 6.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  556 KEAKEKFLhEVVKMRVKQEEKLSA-ALQAKRSLHQ----------ELEFLRVAKKEKLreATEAKRNLRKEIERLRAENE 624
Cdd:cd22656 113 EEAKKTIK-ALLDDLLKEAKKYQDkAAKVVDKLTDfenqtekdqtALETLEKALKDLL--TDEGGAIARKEIKDLQKELE 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  625 KKMKEANEsrlRLKRELEQARqarvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRA------DLLRE-REAREH 697
Cdd:cd22656 190 KLNEEYAA---KLKAKIDELK-------------------ALIADDEAKLAAALRLIADLTAadtdldNLLALiGPAIPA 247


                ....
gi 4506967  698 LEKV 701
Cdd:cd22656 248 LEKL 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
538-689 6.76e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFL--HEVVKMRVKQEEKLSAALQAKRSL---HQELEFLRVAKKEKLREATEAKRNL 612
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEEL 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  613 RKEIERLRAENEKKMKEANES-------RLRLKRELEQARQarvcdkgcEAGRLRakysAQIEDLQVKLQHAEADREQLR 685
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEEleelqqrLAELEEELEEAQE--------ELEELE----EELEQLENELEAAALEERLKE 247


                ....
gi 4506967  686 ADLL 689
Cdd:COG4717 248 ARLL 251
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 599-708 6.90e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  599 KEKLREATEAKRNLRKEIERLRAENEKKMKEANESRlrlKRELEQARQarvcdkgcEAGRLRAKYSAQIEdlqvklqhAE 678
Cdd:cd06503  32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEA---QEIIEEARK--------EAEKIKEEILAEAK--------EE 92

                        90       100       110
                ....*....|....*....|....*....|..
gi 4506967  679 ADR--EQLRADLLRERearehlEKVVKELQEQ 708
Cdd:cd06503  93 AERilEQAKAEIEQEK------EKALAELRKE 118
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
545-709 7.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  545 LRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAK--KEKLREATEAKRNLRkeIERLRAE 622
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEelQELLREAEELEEELQ--LEELEQE 371

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  623 NEKKMKEAN-ESRLRLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDL--QVKLQHAEADREQLRADLLREREAREHLE 699
Cdd:COG4717 372 IAALLAEAGvEDEEELRAALEQAEEYQ------ELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELE 445

                       170
                ....*....|
gi 4506967  700 KVVKELQEQL 709
Cdd:COG4717 446 EELEELREEL 455
mukB PRK04863
chromosome partition protein MukB;
539-695 7.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    539 EAELEHLRQA---LEGGLDTKEAKEKFLHEVV---KMRVKQEEKL--SAALQAKRSLHQELEFLRvakkEKLREATEAKR 610
Cdd:PRK04863  836 EAELRQLNRRrveLERALADHESQEQQQRSQLeqaKEGLSALNRLlpRLNLLADETLADRVEEIR----EQLDEAEEAKR 911

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    611 NLRK------EIER----LRAENE-----KKMKEANESRLRL----KRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQ 671
Cdd:PRK04863  912 FVQQhgnalaQLEPivsvLQSDPEqfeqlKQDYQQAQQTQRDakqqAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLR 991

                         170       180
                  ....*....|....*....|....
gi 4506967    672 VKLQHAEADREQLRaDLLREREAR 695
Cdd:PRK04863  992 QRLEQAEQERTRAR-EQLRQAQAQ 1014
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 612-706 8.52e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 38.92  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    612 LRKEIERLRAENEK----------KMKEANESRLRLKREL-----EQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQH 676
Cdd:pfam15294 131 LHMEIERLKEENEKlkerlktlesQATQALDEKSKLEKALkdlqkEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210

                          90       100       110
                  ....*....|....*....|....*....|....
gi 4506967    677 AEADREQLRADLLRER----EAREHLEKVVKELQ 706
Cdd:pfam15294 211 STALQKSLEEDLASTKhellKVQEQLEMAEKELE 244
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 597-705 8.84e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.46  E-value: 8.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  597 AKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLkreLEQARQarvcdkgcEAGRLRAKYSAQIEdlqvklQH 676
Cdd:COG0711  31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEI---IAEARK--------EAEAIAEEAKAEAE------AE 93

                        90       100       110
                ....*....|....*....|....*....|
gi 4506967  677 AEADREQLRADLLRERE-AREHLEKVVKEL 705
Cdd:COG0711  94 AERIIAQAEAEIEQERAkALAELRAEVADL 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-705 8.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 8.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIE 617
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE----ALEEQLEAEREELLEELLEEE 745

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEKKMKEANESRLRLKRELEQARQARvcdkgcEA-GR--LRAkysaqIEDLQ-VKLQHAEADREqlRADLlreRE 693
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREI------EAlGPvnLLA-----IEEYEeLEERYDFLSEQ--REDL---EE 809

                       170
                ....*....|..
gi 4506967  694 AREHLEKVVKEL 705
Cdd:COG1196 810 ARETLEEAIEEI 821
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-709 9.18e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  538 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 617
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967  618 RLRAENEKKMKEANESRLRLKRELE-QARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRErEARE 696
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEErLEEELE------EEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLE 763

                       170
                ....*....|...
gi 4506967  697 HLEKVVKELQEQL 709
Cdd:COG1196 764 ELERELERLEREI 776
PTZ00121 PTZ00121
MAEBL; Provisional
 543-708 9.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    543 EHLRQALEGgldtKEAKEKFLHEVVKmRVKQEEKLSAALQAK--RSLHQELEFLRVAKKEKLREATEAKR--------NL 612
Cdd:PTZ00121 1137 EDARKAEEA----RKAEDAKRVEIAR-KAEDARKAEEARKAEdaKKAEAARKAEEVRKAEELRKAEDARKaeaarkaeEE 1211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506967    613 RKEIERLRAENEKKMKEANESRlRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADR--------EQL 684
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKadelkkaeEKK 1290

                         170       180
                  ....*....|....*....|....
gi 4506967    685 RADLLREREAREHLEKVVKELQEQ 708
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEA 1314
 
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