NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530360372|ref|XP_005244832|]
View 

ski oncogene isoform X1 [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 1.35e-61

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: 201.45  E-value: 1.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083    1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                         90       100
                 ....*....|....*....|..
gi 530360372 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 3.66e-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: 175.54  E-value: 3.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 530360372  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 ...
 540-711 1.51e-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: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 617
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   618 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 697
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 530360372   698 EHLEKVVKELQEQL 711
Cdd:TIGR02168  368 EELESRLEELEEQL 381
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.60e-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: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 530360372 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 1.35e-61

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: 201.45  E-value: 1.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083    1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                         90       100
                 ....*....|....*....|..
gi 530360372 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 3.66e-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: 175.54  E-value: 3.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 530360372  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 6.66e-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: 175.16  E-value: 6.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   92 MPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSA 171
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90
                  ....*....|....*....
gi 530360372  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 8.53e-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: 174.48  E-value: 8.53e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYtGKEE 296
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 530360372   297 QARLGRCLDDVKEKFD 312
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-711 1.51e-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: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 617
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   618 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 697
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 530360372   698 EHLEKVVKELQEQL 711
Cdd:TIGR02168  368 EELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-729 2.93e-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: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 618
Cdd:COG1196  218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 619 ERLRAE---NEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRERE 695
Cdd:COG1196  298 ARLEQDiarLEERRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530360372 696 AREHLEKVVKELQEQlwpRARPEAAGSEGAAELE 729
Cdd:COG1196  373 ELAEAEEELEELAEE---LLEALRAAAELAAQLE 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
541-709 4.69e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 541 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 619
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 530360372 697 REHLEKVVKELQE 709
Cdd:PRK03918 710 KKELEKLEKALER 722
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 558-711 3.99e-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: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  558 KEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRL 637
Cdd:pfam13868  47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530360372  638 RLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHlEKVVKELQEQL 711
Cdd:pfam13868 127 QLREEIDEFNEEQ------AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRAQQ 193
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.60e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 530360372 466 ETLAP-----VAAPEEDK 478
Cdd:PTZ00449 740 DAEQPddiefFTPPEEER 757
growth_prot_Scy NF041483
polarized growth protein Scy;
605-729 1.65e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  605 REATEAKRNLRKEIERLRAENEKKMK----EANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAE 680
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQAEevraAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372  681 ADREQLRadllreREAREHLEKV-------VKELQ---EQLWPRARPEAAGSEGAAELE 729
Cdd:NF041483  600 AEAERIR------REAAEETERLrteaaerIRTLQaqaEQEAERLRTEAAADASAARAE 652
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 545-607 1.84e-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: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360372 545 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 607
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 1.35e-61

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: 201.45  E-value: 1.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  91 FMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFS 170
Cdd:cd21083    1 FMPSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFS 80

                         90       100
                 ....*....|....*....|..
gi 530360372 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 3.29e-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: 192.10  E-value: 3.29e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  93 PSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAP 172
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90
                 ....*....|....*....
gi 530360372 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 1.27e-57

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: 190.08  E-value: 1.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 100 RCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITK 179
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                         90
                 ....*....|.
gi 530360372 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 3.66e-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: 175.54  E-value: 3.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQdYTGKEE 296
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 530360372  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 6.66e-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: 175.16  E-value: 6.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   92 MPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSA 171
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90
                  ....*....|....*....
gi 530360372  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 8.53e-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: 174.48  E-value: 8.53e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   217 SVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYtGKEE 296
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 530360372   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 1.42e-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: 123.56  E-value: 1.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 103 TVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDA 182
Cdd:cd21074    4 STLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISKSDA 83


                 ....*
gi 530360372 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 1.04e-19

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: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 104 VLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAE 183
Cdd:cd21080    5 ILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAE 84


                 ....*..
gi 530360372 184 RLCNALL 190
Cdd:cd21080   85 RLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-711 1.51e-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: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGgLDTKEAKEK--FLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKE 617
Cdd:TIGR02168  218 LKAELRELELALLV-LRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   618 IERLraenEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 697
Cdd:TIGR02168  297 ISRL----EQQKQILRERLANLERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170
                   ....*....|....
gi 530360372   698 EHLEKVVKELQEQL 711
Cdd:TIGR02168  368 EELESRLEELEEQL 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-729 2.93e-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: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGG-LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 618
Cdd:COG1196  218 LKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 619 ERLRAE---NEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRERE 695
Cdd:COG1196  298 ARLEQDiarLEERRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530360372 696 AREHLEKVVKELQEQlwpRARPEAAGSEGAAELE 729
Cdd:COG1196  373 ELAEAEEELEELAEE---LLEALRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-711 1.91e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKL-----------------SAALQAKRSLHQELEFLRVAKKE 602
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeleekleelkeeleslEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   603 KLREATEAKRNLRKEIERLRAE---NEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHA 679
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          170       180       190
                   ....*....|....*....|....*....|..
gi 530360372   680 EADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
543-712 5.93e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 543 ELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL-----RVAKKEKLREATEAKRNLRKE 617
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 618 IERLRaENEKKMKEANESRLRLKRELEQARQarvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR 697
Cdd:COG4717  155 LEELR-ELEEELEELEAELAELQEELEELLE-----------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                        170
                 ....*....|....*
gi 530360372 698 EHLEKVVKELQEQLW 712
Cdd:COG4717  223 EELEEELEQLENELE 237
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 103-187 1.39e-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: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 103 TVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDA 182
Cdd:cd21082    4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDV 83


                 ....*
gi 530360372 183 ERLCN 187
Cdd:cd21082   84 ERLYS 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 575-711 2.22e-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: 54.68  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   575 QEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKkmkeANESRLRLKRELEQARQARvcdk 654
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEI---- 763

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530360372   655 gceagrlrAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:TIGR02168  764 --------EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
541-709 4.69e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 541 EAELEHLRQALEGGLDTKEAK-EKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRnLRKEIE 619
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEANESRLR---LKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:PRK03918 630 KAFEELAETEKRLEELRKEleeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709

                        170
                 ....*....|...
gi 530360372 697 REHLEKVVKELQE 709
Cdd:PRK03918 710 KKELEKLEKALER 722
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-711 4.95e-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: 4.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFL---RVAKKEKLREATEAKRNLRK 616
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   617 EIERLRAENEKKMKEANESRLRLKRELEQARQARvcDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                          170
                   ....*....|....*
gi 530360372   697 REHLEKVVKELQEQL 711
Cdd:TIGR02168  861 IEELEELIEELESEL 875
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 574-711 5.90e-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: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 574 KQEEKLSA-ALQAKRslHQEL-EFLRVAKKE----KLREATEAKRNLRKEIERLRAENEKKMK-----EANESRLRLKRE 642
Cdd:COG1196  200 RQLEPLERqAEKAER--YRELkEELKELEAEllllKLRELEAELEELEAELEELEAELEELEAelaelEAELEELRLELE 277

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372 643 LEQARQArvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:COG1196  278 ELELELE-------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 540-729 6.34e-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: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIE 619
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEA--------------------NESRLRLKRELEQARQARVcdkgceagrlrAKYSAQIEDLQVKLQHA 679
Cdd:COG4942  101 AQKEELAELLRALyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQA-----------EELRADLAELAALRAEL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530360372 680 EADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
539-729 7.48e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  539 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 618
Cdd:COG4913   239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  619 ERLRAE---NEKKMKEANESRL-RLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKlqhAEADREQLRADLLRER 694
Cdd:COG4913   319 DALREEldeLEAQIRGNGGDRLeQLEREIERLERELE-----ERERRRARLEALLAALGLP---LPASAEEFAALRAEAA 390

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530360372  695 EAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
Cdd:COG4913   391 ALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-730 1.38e-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: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLHEVvKMRVKQeekLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 619
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDEL-RAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   620 RLRAENEKKMKEANESRLRLKRELEQARQARVCDKgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 699
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALA--LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170       180       190
                   ....*....|....*....|....*....|.
gi 530360372   700 LEKVVKELQEQLWPRARPEAagsEGAAELEP 730
Cdd:TIGR02168  934 LEVRIDNLQERLSEEYSLTL---EEAEALEN 961
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
549-711 1.46e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 549 QALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKK--EKLREATEAKRNLRKEIERLRA--E 624
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEEleE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 625 NEKKMKEANESRLRLKRELEQARQARVcdkgceagRLRAKYSAQIEDlqvKLQHAEADREQLRADLLREREAREHLEKVV 704
Cdd:COG4717  154 RLEELRELEEELEELEAELAELQEELE--------ELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEEL 222


                 ....*..
gi 530360372 705 KELQEQL 711
Cdd:COG4717  223 EELEEEL 229
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 578-711 1.54e-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: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 578 KLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcdkgce 657
Cdd:COG1579   18 ELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK------- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530360372 658 agrlrakysaQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:COG1579   90 ----------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
572-729 2.39e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.64  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 572 RVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAkrNLRKEIERLRAENEKKMKEANESRLR-LKRELEQARQAR 650
Cdd:COG2268  213 EIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA--EERREAETARAEAEAAYEIAEANAEReVQRQLEIAERER 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372 651 vcdkgceagrlrakysaqiedlQVKLQHAEADREQLRADllREREAREHLEKVVKELQEqlwpRARPEAAGSEGAAELE 729
Cdd:COG2268  291 ----------------------EIELQEKEAEREEAELE--ADVRKPAEAEKQAAEAEA----EAEAEAIRAKGLAEAE 341
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
540-711 2.63e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKF--LHEVVKMRVKQEEKLSAAL--QAKRSLHQELEFLRVAKKE---KLREATEAKR 612
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERheLYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEieeEISKITARIG 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 613 NLRKEIERLRaENEKKMKEANESRLRLKRELEQArqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR 692
Cdd:PRK03918 416 ELKKEIKELK-KAIEELKKAKGKCPVCGRELTEE----------HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484

                        170       180
                 ....*....|....*....|.
gi 530360372 693 EREAREHLEKVVK--ELQEQL 711
Cdd:PRK03918 485 LEKVLKKESELIKlkELAEQL 505
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
540-711 3.05e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSaalQAKRSLHQELEFLRVAKkEKLREATEAKRNLRKEIE 619
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE---ELNEQLQAAQAELAQAQ-EELESLQEEAEELQEELE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEANESRLRLKrELEQARQARvcdkgceagrlrakySAQIEDLQVKLQHAEADREQLRADL--LREREAR 697
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIA-ELQSEIAER---------------EEELKELEEQLESLQEELAALEQELqaLSEAEAE 182

                        170
                 ....*....|....
gi 530360372 698 EHLEKVVKELQEQL 711
Cdd:COG4372  183 QALDELLKEANRNA 196
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
558-709 4.06e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.24  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 558 KEAKEKFLHEVVKMRVKQEEKLSAALQAKR-----SLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAEN---EKKM 629
Cdd:COG2433  357 KKVPPDVDRDEVKARVIRGLSIEEALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeelEAEL 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 630 KEANESRLRLKRELEQARQARvcdkgceagRLRAKYSAQIEDLQVKLqhaeadrEQLRADLLREREAREHLEKVVKELQE 709
Cdd:COG2433  437 EEKDERIERLERELSEARSEE---------RREIRKDREISRLDREI-------ERLERELEEERERIEELKRKLERLKE 500
PTZ00121 PTZ00121
MAEBL; Provisional
 540-723 5.07e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGGLDTKEAKEKflheVVKMRVKQEEKLSAALQAKRSLHQELEFLRVA----KKEKLREATEAKR--- 612
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKKade 1550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  613 -----NLRKEIERLRAENEKKMKEANESRLRLKRELEQARQAR---VCDKGCEAGRLRAKYSAQIEDLQVK---LQHAEA 681
Cdd:PTZ00121 1551 lkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieeVMKLYEEEKKMKAEEAKKAEEAKIKaeeLKKAEE 1630

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530360372  682 DREQLRADLLREREAREHLEKVVKElQEQLWPRARPEAAGSE 723
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAE 1671
PTZ00121 PTZ00121
MAEBL; Provisional
 540-705 1.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGGLDTKEAKEKflHEVVKmrvKQEEKLSAALQAKRSLHQELEFLRVAKK-EKLREATEAKRnlrKEI 618
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKK--ADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKK---KAE 1454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  619 ERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 698
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534


                  ....*..
gi 530360372  699 HLEKVVK 705
Cdd:PTZ00121 1535 KADEAKK 1541
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
542-711 1.34e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 542 AELEHLRQALEGGLDTKEAKekflHEVVKMRVKQEEKLSAaLQAKRSLHQELeflRVAKKEKLREATEAKRNLRKEIERL 621
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEER----LERAEDLVEAEDRIER-LEERREDLEEL---IAERRETIEEKRERAEELRERAAEL 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 622 RAENEKKMKEANESRlrlkrelEQARQARVCDKGCEagRLRAKYSAQIEDLQvKLQHAEADREQLRADLLREREAREHLE 701
Cdd:PRK02224 550 EAEAEEKREAAAEAE-------EEAEEAREEVAELN--SKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALA 619

                        170
                 ....*....|
gi 530360372 702 KVVKELQEQL 711
Cdd:PRK02224 620 ELNDERRERL 629
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
544-729 1.97e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 544 LEHLRQALEGGLDtKEAKEKF-----LHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEI 618
Cdd:COG4717   40 LAFIRAMLLERLE-KEADELFkpqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 619 ERLR-----AENEKKMKEANESRLRLKRELEQARQARvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADLLRE 693
Cdd:COG4717  119 EKLEkllqlLPLYQELEALEAELAELPERLEELEERL----------------EELRELEEELEELEAELAELQEELEEL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530360372 694 RE-----AREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
Cdd:COG4717  183 LEqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-700 2.21e-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: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEgglDTKEAKEKFLHEVVKMRVkQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 619
Cdd:TIGR02168  836 TERRLEDLEEQIE---ELSEDIESLAAEIEELEE-LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   620 RLRAENEKKMKEANESRLRLKR-ELEQARQarvcdkgceAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREARE 698
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGlEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 530360372   699 HL 700
Cdd:TIGR02168  983 EL 984
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 540-711 3.56e-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: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLR---- 615
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKeyea 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 616 --KEIERLRAEN---EKKMKEANESRLRLKRELEQARqarvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRADL 690
Cdd:COG1579   94 lqKEIESLKRRIsdlEDEILELMERIEELEEELAELE-------------------AELAELEAELEEKKAELDEELAEL 154

                        170       180
                 ....*....|....*....|..
gi 530360372 691 LREREA-REHLEKVVKELQEQL 711
Cdd:COG1579  155 EAELEElEAEREELAAKIPPEL 176
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 558-711 3.99e-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: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  558 KEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRL 637
Cdd:pfam13868  47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530360372  638 RLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHlEKVVKELQEQL 711
Cdd:pfam13868 127 QLREEIDEFNEEQ------AEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-EREIARLRAQQ 193
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
574-711 4.41e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 574 KQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAEnekkMKEANESRLRLKRELEQARQArvcd 653
Cdd:COG4372    3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREE----LEQAREELEQLEEELEQARSE---- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530360372 654 kgceagrlRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:COG4372   75 --------LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 539-709 4.43e-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: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   539 GLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAK-RSLHQELEFLRVAKKEKLREATEAKRNLRK- 616
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKl 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   617 --EIERLRAENEKkmkeanesrlrLKRELEQaRQARVCDKGCEAGRLRAKYsaqiEDLQVKLQHAEADREQLRADLlreR 694
Cdd:TIGR02169  328 eaEIDKLLAEIEE-----------LEREIEE-ERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDEL---K 388

                          170
                   ....*....|....*
gi 530360372   695 EAREHLEKVVKELQE 709
Cdd:TIGR02169  389 DYREKLEKLKREINE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
540-711 4.62e-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: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGgLDTKEA---KEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEkLREATEAKRNLRK 616
Cdd:COG4913   622 LEEELAEAEERLEA-LEAELDalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD-LAALEEQLEELEA 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  617 EIERLRAEnekkMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:COG4913   700 ELEELEEE----LDELKGEIGRLEKELEQAEE-------------------ELDELQDRLEAAEDLARLELRALLEERFA 756

                         170
                  ....*....|....*
gi 530360372  697 REHLEKVVKELQEQL 711
Cdd:COG4913   757 AALGDAVERELRENL 771
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
576-716 5.07e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 576 EEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcdkg 655
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ----- 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360372 656 ceagrlrakysAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRAR 716
Cdd:COG4372  101 -----------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
PRK12704 PRK12704
phosphodiesterase; Provisional
 571-710 5.87e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 571 MRVKQEEKLSAA-LQAKRSLHQELEFLRVAKKEKLREATEakrnlrkEIERLRAENEKKMKEAN------ESRLRLKREL 643
Cdd:PRK12704  25 RKKIAEAKIKEAeEEAKRILEEAKKEAEAIKKEALLEAKE-------EIHKLRNEFEKELRERRnelqklEKRLLQKEEN 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360372 644 EQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR-----EREAREH-LEKVVKELQEQ 710
Cdd:PRK12704  98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEIlLEKVEEEARHE 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
542-711 1.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 542 AELEHLRQALEGGLDTKEAKEKFLHEVVKmRVKQeeklsaaLQAKRSLHQELEFLRVAKKEKLREATEAK---RNLRKEI 618
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVK-ELKE-------LKEKAEEYIKLSEFYEEYLDELREIEKRLsrlEEEINGI 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 619 ERLRAENEKKMKEANESRLRLK-------------RELEQARQarvcdKGCEAGRLRAKYSA-QIEDLQVKLQHAEADRE 684
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKelekrleeleerhELYEEAKA-----KKEELERLKKRLTGlTPEKLEKELEELEKAKE 401

                        170       180
                 ....*....|....*....|....*..
gi 530360372 685 QLRADLLREREAREHLEKVVKELQEQL 711
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAI 428
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 612-710 1.73e-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: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  612 RNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakysaQIEDLQVKLQHAEADREQLRA 688
Cdd:pfam13851  29 KSLKEEIAELKkkeERNEKLMSEIQQENKRLTEPLQKAQE-------------------EVEELRKQLENYEKDKQSLKN 89

                          90       100
                  ....*....|....*....|..
gi 530360372  689 dlLREReaREHLEKVVKELQEQ 710
Cdd:pfam13851  90 --LKAR--LKVLEKELKDLKWE 107
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-728 2.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIE 619
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEA 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEkkmkEANESRLRLKRELEQARQArvcdkgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREH 699
Cdd:COG1196  453 ELEEEEE----ALLELLAELLEEAALLEAA----------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                        170       180
                 ....*....|....*....|....*....
gi 530360372 700 LEKVVKELQEQLWPRARPEAAGSEGAAEL 728
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 ...
 540-718 2.33e-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: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEK-LSAALQAKRSLHQELEFLRVAKKEKLREATEAKRN---LR 615
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKeNKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvdDE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   616 KEIERLRAENEKKMKEAN---ESRLRLKRELEqarqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLR 692
Cdd:pfam02463  314 EKLKESEKEKKKAEKELKkekEEIEELEKELK------------ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381

                          170       180
                   ....*....|....*....|....*.
gi 530360372   693 EreaREHLEKVVKELQEQLWPRARPE 718
Cdd:pfam02463  382 E---SERLSSAAKLKEEELELKSEEE 404
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 542-711 2.53e-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: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  542 AELEHLRQALEGGLdtkEAKEKFLHEVVKMRVKQeeklsAALQAKRSLHQE----LEFLRVAkkEKLREATEAKRNLRKE 617
Cdd:pfam09727   5 DDLLKLLSILEGEL---QARDIVIAVLKAEKVKQ-----LLLEARYGFKYPsdplLALQRDS--ELLRDQSQDEDVYEAM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  618 IERLRAENEKKMKEANESRLRLKRELEQA--RQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHaeaDREQLRADLLRERE 695
Cdd:pfam09727  75 YEKPLAELEKLVEKQRETQRRMLEQLAAAekRHRRVIRELEEEKRKHARDTAQGDDFTYLLEK---ERERLKQELEQEKA 151

                         170
                  ....*....|....*.
gi 530360372  696 AREHLEKVVKELQEQL 711
Cdd:pfam09727 152 QQKRLEKELKKLLEKL 167
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
558-709 2.75e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 558 KEAKEKF---LHEVVKMRvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLR------KEIERLRAENEKK 628
Cdd:PRK03918 196 KEKEKELeevLREINEIS-SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 629 MKEANESRLRLK---------RELEQARQARVcDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAR-- 697
Cdd:PRK03918 275 IEELEEKVKELKelkekaeeyIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkr 353

                        170
                 ....*....|...
gi 530360372 698 -EHLEKVVKELQE 709
Cdd:PRK03918 354 lEELEERHELYEE 366
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 541-710 2.87e-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: 44.33  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  541 EAELEHLRQALEggldtkeAKEKFLHEVvkmrvKQEEKLSAALQAKRslhQELEFLRVAKKEKLRE-------ATEAKRN 613
Cdd:pfam05483 404 EVELEELKKILA-------EDEKLLDEK-----KQFEKIAEELKGKE---QELIFLLQAREKEIHDleiqltaIKTSEEH 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  614 LRKEIERLRAENEK-KMKE----ANESRLRLK-RELEQarqarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLR 687
Cdd:pfam05483 469 YLKEVEDLKTELEKeKLKNieltAHCDKLLLEnKELTQ-----------EASDMTLELKKHQEDIINCKKQEERMLKQIE 537

                         170       180
                  ....*....|....*....|...
gi 530360372  688 ADLLREREAREHLEKVVKELQEQ 710
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQK 560
PTZ00121 PTZ00121
MAEBL; Provisional
 543-710 2.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  543 ELEHLRQALEGGLDTKEAKEKFLHEVvkMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRN-----LRKE 617
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeaeeKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  618 IERLRAENEKKMKEANESRL--RLKRELEQARQARVCD-KGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADllrER 694
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEkKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EE 1726

                         170
                  ....*....|....*.
gi 530360372  695 EAREHLEKVVKELQEQ 710
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEED 1742
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 540-709 2.93e-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: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLhevVKMRVKQEEKLSAALQAKRSLHQELEFL--RVAKKEKLREATEAKRN-LRK 616
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALERQKEAIerQLASLEEELEKLTEEISeLEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   617 EIE----RLRAENEKKMKEANESRLRLKRELE--QARQARVCDKGCEAGR--------------LRAKYSAQIEDLQVKL 676
Cdd:TIGR02169  266 RLEeieqLLEELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIAEKEReledaeerlakleaEIDKLLAEIEELEREI 345

                          170       180       190
                   ....*....|....*....|....*....|...
gi 530360372   677 QHAEADREQLRADLlreREAREHLEKVVKELQE 709
Cdd:TIGR02169  346 EEERKRRDKLTEEY---AELKEELEDLRAELEE 375
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 574-706 3.46e-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: 41.01  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  574 KQEEKLSAALQAKRSLHQELEflrvakkeklREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARvcd 653
Cdd:pfam13863   6 REMFLVQLALDAKREEIERLE----------ELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEET--- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530360372  654 kgceagRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKE 706
Cdd:pfam13863  73 ------KLKKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEKVVPK 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 540-711 3.47e-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: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGgLDTKEAKEKFLHEVVKMRVKQ-EEKLSAALQAKRSLHQELEFLRvAKKEKLREATEA-------- 610
Cdd:TIGR02169  714 ASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSlEQEIENVKSELKELEARIEELE-EDLHKLEEALNDlearlshs 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   611 ----KRNLRKEIERLRAENEKKMKEAN--ESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADRE 684
Cdd:TIGR02169  792 ripeIQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                          170       180
                   ....*....|....*....|....*..
gi 530360372   685 QLRADLLREREAREHLEKVVKELQEQL 711
Cdd:TIGR02169  872 ELEAALRDLESRLGDLKKERDELEAQL 898
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 591-724 3.49e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 591 QELEFLRVAKKEKLREATEakrnLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVcdkgCEAGRLRAKYSAQIE 670
Cdd:PRK00409 523 ASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI----KEAKKEADEIIKELR 594

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530360372 671 DLQvKLQHAEADREQLradllreREAREHLEKVVKELQEQLWPRARPEAAGSEG 724
Cdd:PRK00409 595 QLQ-KGGYASVKAHEL-------IEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
PTZ00121 PTZ00121
MAEBL; Provisional
 558-727 4.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  558 KEAKEKFLHEVVKmrvKQEEKLSAALQAKRSLHQEleflrVAKKEKLREATEAKRnLRKEIERLRAENEKK----MKEAN 633
Cdd:PTZ00121 1614 KAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEE-----KKKAEELKKAEEENK-IKAAEEAKKAEEDKKkaeeAKKAE 1684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  634 ESRLR----LKRELEQARQARVCDKGCEAGRLRA---KYSAQIEDLQVKLQHAEADREQLRADLLR----EREAREHLEK 702
Cdd:PTZ00121 1685 EDEKKaaeaLKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeeEKKKIAHLKK 1764

                         170       180
                  ....*....|....*....|....*
gi 530360372  703 VVKELQEQLwpRARPEAAGSEGAAE 727
Cdd:PTZ00121 1765 EEEKKAEEI--RKEKEAVIEEELDE 1787
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 101-185 5.65e-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: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 101 CETV-LEGETISCFVVGGEKRLCLPQILNSVLRDF--SLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLI 177
Cdd:cd21081    3 CKMVeYRGAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLI 82


                 ....*...
gi 530360372 178 TKTDAERL 185
Cdd:cd21081   83 SRKDFDTL 90
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 542-711 5.68e-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: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  542 AELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAK----RSLHQELEFLRVAKKEK---LREATEAKRNL 614
Cdd:pfam05557  30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaelnRLKKKYLEALNKKLNEKesqLADAREVISCL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  615 RKEIERLRAENEKKMKEANESRLRLK--RELEQARQARVcdkgceagrlrAKYSAQIEDLQVKlQHAEADREQLRADLLR 692
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEelQERLDLLKAKA-----------SEAEQLRQNLEKQ-QSSLAEAEQRIKELEF 177

                         170
                  ....*....|....*....
gi 530360372  693 EREAREHLEKVVKELQEQL 711
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSEL 196
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 557-711 6.18e-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: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   557 TKEAK--EKFLHEVVKMRVKQEEKlSAALQAKRSLHQ----ELEfLRVAKKEKLREATE-AKRNLRKEIERLRAENEKKM 629
Cdd:pfam01576  151 SKERKllEERISEFTSNLAEEEEK-AKSLSKLKNKHEamisDLE-ERLKKEEKGRQELEkAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   630 KEANESRLRL-KRELE-QARQARVCDKGceagrlrakysAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKEL 707
Cdd:pfam01576  229 AQIAELRAQLaKKEEElQAALARLEEET-----------AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297


                   ....
gi 530360372   708 QEQL 711
Cdd:pfam01576  298 GEEL 301
PRK11020 PRK11020
YibL family ribosome-associated protein;
571-649 6.46e-04

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 40.01  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 571 MRVKQE-EKLSAALQAKRslHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKM-KEANE-SRLRLKRELEQAR 647
Cdd:PRK11020   1 MVEKNEiKRLSDRLDAIR--HKLAAASLRGDAEKYAQFEKEKATLEAEIARLKEVQSQKLsKEAQKlMKLPFSRAITKKE 78


                 ..
gi 530360372 648 QA 649
Cdd:PRK11020  79 QA 80
PTZ00121 PTZ00121
MAEBL; Provisional
 545-702 7.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  545 EHLRQALEGGLDTKEAKEKFLHEVVK---MRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERL 621
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  622 RAENEKKMKEANESRLRLKRELEQARQARV--CDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA--R 697
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviE 1782


                  ....*
gi 530360372  698 EHLEK 702
Cdd:PTZ00121 1783 EELDE 1787
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 540-711 8.92e-04

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: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGGL-DTKEAKEKFLHEVVKMrvkqeeklsaalqakrsLHQELEFLRvakkEKLREATEAKRN-LRKE 617
Cdd:pfam01442  31 LEKETEALRERLQKDLeEVRAKLEPYLEELQAK-----------------LGQNVEELR----QRLEPYTEELRKrLNAD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  618 IERLRAENEKKMKEANEsrlRLKRELEQARqARVcdkGCEAGRLRAKYSAQIEDLQVKLQ-HAEADREQLRadlLREREA 696
Cdd:pfam01442  90 AEELQEKLAPYGEELRE---RLEQNVDALR-ARL---APYAEELRQKLAERLEELKESLApYAEEVQAQLS---QRLQEL 159

                         170
                  ....*....|....*
gi 530360372  697 REHLEKVVKELQEQL 711
Cdd:pfam01442 160 REKLEPQAEDLREKL 174
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
540-711 9.24e-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: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGGldTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNL-RKEI 618
Cdd:COG4913   267 ARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR----EELDELEAQIRGNgGDRL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  619 ERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAG---------RLRAKYSAQIEDLQVKLQHAEADREQLRAD 689
Cdd:COG4913   341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalraeaaALLEALEEELEALEEALAEAEAALRDLRRE 420

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530360372  690 L------LREREAR-----EHLEKVVKELQEQL 711
Cdd:COG4913   421 LreleaeIASLERRksnipARLLALRDALAEAL 453
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 578-729 9.80e-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: 42.75  E-value: 9.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   578 KLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANesRLRLKRELEQARQARVCDKGCE 657
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530360372   658 AGRLRAKYSAQIEDLQVKLQHAEADREQLRADL--LREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 545-723 1.17e-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: 42.42  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  545 EHLRQALEGG----LDTKEAKEKFLHEVVKM---RVKQEEKLSAALQA---------KRSLHQELEflRVAKKEKLREAT 608
Cdd:pfam17380 392 ERVRQELEAArkvkILEEERQRKIQQQKVEMeqiRAEQEEARQREVRRleeeraremERVRLEEQE--RQQQVERLRQQE 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  609 EAKRNLRKEIERlraENEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADR---EQ 685
Cdd:pfam17380 470 EERKRKKLELEK---EKRDRKRAEEQRRKILEKELEERKQAMI-----EEERKRKLLEKEMEERQKAIYEEERRReaeEE 541

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 530360372  686 LRADllREREAREHLEKVVKELQEQlwpRARPEAAGSE 723
Cdd:pfam17380 542 RRKQ--QEMEERRRIQEQMRKATEE---RSRLEAMERE 574
Filament pfam00038
Intermediate filament protein;
572-711 1.17e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.83  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  572 RVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATeaKRNLRKEIERLRAEnekkmkeanesRLRLKRELEQARQArv 651
Cdd:pfam00038  19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKE--IEDLRRQLDTLTVE-----------RARLQLELDNLRLA-- 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  652 cdkgceAGRLRAKYsaqiEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:pfam00038  84 ------AEDFRQKY----EDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEEL 133
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 540-711 1.27e-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: 42.47  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAElEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLsaalQAKRSLHQEleflRVAKKE-KLREATEAKRNLRKei 618
Cdd:pfam01576  112 LDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL----SKERKLLEE----RISEFTsNLAEEEEKAKSLSK-- 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   619 erLRAENEKKMKEANEsrlRLKRElEQARQARVCDK---GCEAGRLR---AKYSAQIEDLQVKLQHAEADREQLRADLLR 692
Cdd:pfam01576  181 --LKNKHEAMISDLEE---RLKKE-EKGRQELEKAKrklEGESTDLQeqiAELQAQIAELRAQLAKKEEELQAALARLEE 254

                          170
                   ....*....|....*....
gi 530360372   693 EREAREHLEKVVKELQEQL 711
Cdd:pfam01576  255 ETAQKNNALKKIRELEAQI 273
mukB PRK04863
chromosome partition protein MukB;
558-720 1.32e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  558 KEAKEKFLHEVVKMRVKQE--EKLSAALQAKRSLHQELEflRVAKKEKLREATEAKRNLRKEIERLRAEnEKKMKEAnES 635
Cdd:PRK04863  452 QEATEELLSLEQKLSVAQAahSQFEQAYQLVRKIAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQL-RMRLSEL-EQ 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  636 RLRLKRELEQA------RQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKvvkelQE 709
Cdd:PRK04863  528 RLRQQQRAERLlaefckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-----RA 602

                         170
                  ....*....|.
gi 530360372  710 QLWPRARPEAA 720
Cdd:PRK04863  603 PAWLAAQDALA 613
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 540-726 1.34e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQ---ALEGGLDTKEAKEKFLHEVVKMRVKQEEK-------LSAALQAKrSLHqelEFL-RVAKKEKL---- 604
Cdd:COG3883   56 LQAELEALQAeidKLQAEIAEAEAEIEERREELGERARALYRsggsvsyLDVLLGSE-SFS---DFLdRLSALSKIadad 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 605 REATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADRE 684
Cdd:COG3883  132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-----EQEALLAQLSAEEAAAEAQLAELEAELA 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530360372 685 QLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAA 726
Cdd:COG3883  207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 598-715 1.36e-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: 40.32  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  598 VAKKEKLRE-----ATEAKRNLRKEIERLRAENEKKMKEANEsrlRLKRELEQARQARvcdkGCEAGRLRAKYSAQIEDL 672
Cdd:pfam01442  10 STYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRA---KLEPYLEELQAKL----GQNVEELRQRLEPYTEEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530360372  673 QVKLqhaEADREQLRADLL-REREAREHLEKVVKELQEQLWPRA 715
Cdd:pfam01442  83 RKRL---NADAEELQEKLApYGEELRERLEQNVDALRARLAPYA 123
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 540-709 1.45e-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: 40.66  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQaleggldTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvAKKEKLREATEAKRNLRKEIE 619
Cdd:pfam13851  31 LKEEIAELKK-------KEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYE-KDKQSLKNLKARLKVLEKELK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  620 RLRAENE-KKMKeanesrlrlKRELEQARQArvcdkgceagrLRAKYSAQIEDLQvklQHAEadreqLRADLLRER--EA 696
Cdd:pfam13851 103 DLKWEHEvLEQR---------FEKVERERDE-----------LYDKFEAAIQDVQ---QKTG-----LKNLLLEKKlqAL 154

                         170
                  ....*....|...
gi 530360372  697 REHLEKVVKELQE 709
Cdd:pfam13851 155 GETLEKKEAQLNE 167
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
604-729 1.56e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.78  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 604 LREATEAKRNLRKEIERLRAENEKKMKEAN----ESRLRLKRELEQARQARvcdKGCEAGRLRAKY-----SAQIE-DLQ 673
Cdd:COG2268  191 RRKIAEIIRDARIAEAEAERETEIAIAQANreaeEAELEQEREIETARIAE---AEAELAKKKAEErreaeTARAEaEAA 267

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360372 674 VKLQHAEADREQLRADLLRERE-----AREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
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 ...
 570-711 1.58e-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: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   570 KMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLR----KEIERLRAENEKKMKE--ANESRLRLKREL 643
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELEEEYLLYLDYlkLNEERIDLLQEL 245

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530360372   644 EQARQAR----------VCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:pfam02463  246 LRDEQEEiesskqeiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 318-478 1.60e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 318 KRRVPRVSSEPPASIRPKTDD--TSSQSPA-PSEKDKPSSWLRTLAGSSNKSlgCVHPRQRLSAFRPWSPAVSASEKE-L 393
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQrpTRPKSPKlPELLDIPKSPKRPESPKSPKR--PPPPQRPSSPERPEGPKIIKSPKPpK 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 394 SPHLP--ALIRDSFY-SY-----KSFETAVAPNVALAPPAQQKvVSSPPCAAAVSRAPEPLATcTQPRKRKLTVDTPGAP 465
Cdd:PTZ00449 662 SPKPPfdPKFKEKFYdDYldaaaKSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPP-KLPRDEEFPFEPIGDP 739

                        170
                 ....*....|....*...
gi 530360372 466 ETLAP-----VAAPEEDK 478
Cdd:PTZ00449 740 DAEQPddiefFTPPEEER 757
PTZ00121 PTZ00121
MAEBL; Provisional
 541-709 1.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  541 EAELEHLRQALEGGLDTKEAKeKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRvaKKEKLREATEakrnLRKEIER 620
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR--KADELKKAEE----KKKADEA 1295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  621 LRAENEKKMKEAnesrlrlKRELEQARQARVCDKGCEAGRLRA------------KYSAQIEDLQVKLQHAEADREQLRA 688
Cdd:PTZ00121 1296 KKAEEKKKADEA-------KKKAEEAKKADEAKKKAEEAKKKAdaakkkaeeakkAAEAAKAEAEAAADEAEAAEEKAEA 1368

                         170       180
                  ....*....|....*....|.
gi 530360372  689 DLLREREAREHLEKVVKELQE 709
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEE 1389
growth_prot_Scy NF041483
polarized growth protein Scy;
605-729 1.65e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  605 REATEAKRNLRKEIERLRAENEKKMK----EANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAE 680
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQAEevraAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372  681 ADREQLRadllreREAREHLEKV-------VKELQ---EQLWPRARPEAAGSEGAAELE 729
Cdd:NF041483  600 AEAERIR------REAAEETERLrteaaerIRTLQaqaEQEAERLRTEAAADASAARAE 652
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 375-483 1.78e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 375 RLSAFRPWSPAVSASEKELSPHLPAlirdsfysyksfeTAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRK 454
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARP-------------EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV 426

                         90       100
                 ....*....|....*....|....*....
gi 530360372 455 RKLTVDTPGAPETLAPVAAPEEDKDSEAE 483
Cdd:PRK14951 427 AAPAAAAPAAAPAAAPAAVALAPAPPAQA 455
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
540-721 1.81e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAAL----------QAKRSLHQELEFLRVAKKEKLREATE 609
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglddadaEAVEARREELEDRDEELRDRLEECRV 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 610 AKRNLRKEIERLR---AENEKKMKEANESRLRLKRELEQARQArVCDKGCEAGRLRAKY---SAQIEDLQVKLQHAEADR 683
Cdd:PRK02224 336 AAQAHNEEAESLRedaDDLEERAEELREEAAELESELEEAREA-VEDRREEIEELEEEIeelRERFGDAPVDLGNAEDFL 414

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530360372 684 EQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAG 721
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALLEAG 452
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 572-729 1.83e-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: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  572 RVKQEEKLSAALQAKRSLHQ-ELEFLRvAKKEKLREATEAKRNLRKEIERLRAEnekkmkeanESRLRLKRELEQARQAr 650
Cdd:pfam05557   1 RAELIESKARLSQLQNEKKQmELEHKR-ARIELEKKASALKRQLDRESDRNQEL---------QKRIRLLEKREAEAEE- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372  651 vcdkgceagrlraKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELE 729
Cdd:pfam05557  70 -------------ALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 545-607 1.84e-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: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360372 545 EHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQE----LEFLRVAKKEKLREA 607
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQatqiLQQVTVKLEDRIREA 223
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 576-678 2.07e-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: 41.70  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   576 EEKLSAALQAKRSLH---QELEFLRVAKKEKLREATEAKRNLRKEIERLRA---ENEKKMKE-------ANESRLRLKRE 642
Cdd:pfam01576  474 QELLQEETRQKLNLStrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlsDMKKKLEEdagtleaLEEGKKRLQRE 553

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 530360372   643 LEQARQaRVCDKGCEAGRL---RAKYSAQIEDLQVKLQH 678
Cdd:pfam01576  554 LEALTQ-QLEEKAAAYDKLektKNRLQQELDDLLVDLDH 591
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 540-709 2.07e-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: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLR---QALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELeflrvakKEKLREATEAKRNLRK 616
Cdd:TIGR02169  327 LEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET-------RDELKDYREKLEKLKR 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   617 EIERLRAENEKKMKEANesrlRLKRELEQARQARvcdKGCEAGrlRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:TIGR02169  400 EINELKRELDRLQEELQ----RLSEELADLNAAI---AGIEAK--INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          170
                   ....*....|....*..
gi 530360372   697 ----REHLEKVVKELQE 709
Cdd:TIGR02169  471 lydlKEEYDRVEKELSK 487
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 543-710 2.31e-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: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  543 ELEHLRQALEGGLDTKEAKEKFLHEVVKMRvkqeeklsaALQAKRSLHQELEflrVAKKEKLREATEAKRNLRKEIE--- 619
Cdd:pfam05557  22 ELEHKRARIELEKKASALKRQLDRESDRNQ---------ELQKRIRLLEKRE---AEAEEALREQAELNRLKKKYLEaln 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  620 RLRAENEKKMKEANESRLRLKRELEQARQarvcdkgceagrlrakySAQIEDLQVKLQHAEADREQLRADLLRER----- 694
Cdd:pfam05557  90 KKLNEKESQLADAREVISCLKNELSELRR-----------------QIQRAELELQSTNSELEELQERLDLLKAKaseae 152

                         170
                  ....*....|....*.
gi 530360372  695 EAREHLEKVVKELQEQ 710
Cdd:pfam05557 153 QLRQNLEKQQSSLAEA 168
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 555-712 2.47e-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: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  555 LDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKR----SLHQELEFLRVAKKEKLREATEAKrNLRKEIERLRAENEKKMK 630
Cdd:pfam14988  28 VQECEEIERRRQELASRYTQQTAELQTQLLQKEkeqaSLKKELQALRPFAKLKESQEREIQ-DLEEEKEKVRAETAEKDR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  631 EANESRLRLKRELE-QARQARVCDKGcEAGRLRAKYSAQIEDLQVKLQHAEADR------EQLRADLL-------REREA 696
Cdd:pfam14988 107 EAHLQFLKEKALLEkQLQELRILELG-ERATRELKRKAQALKLAAKQALSEFCRsikrenRQLQKELLqliqetqALEAI 185

                         170
                  ....*....|....*.
gi 530360372  697 REHLEKVVKELQEQLW 712
Cdd:pfam14988 186 KSKLENRKQRLKEEQW 201
PRK12472 PRK12472
hypothetical protein; Provisional
 575-696 2.49e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.01  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 575 QEEKLSAALQAKRslhqeleflrvAKKEKLREATEAKRNLRKeIERLRAENEKKMKEANESRLRLKRELEQARqarvcdk 654
Cdd:PRK12472 199 AEDAARAADEAKT-----------AAAAAAREAAPLKASLRK-LERAKARADAELKRADKALAAAKTDEAKAR------- 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530360372 655 gceAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREA 696
Cdd:PRK12472 260 ---AEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEA 298
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
546-710 2.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 546 HLRQA-LEGGLDTKEAKEKFLHEVVKMrvkqeEKLSAALQAKRSLHQELEFlRVAKKEKLREATEAKRNLRKEIERLRAE 624
Cdd:PRK03918 131 YIRQGeIDAILESDESREKVVRQILGL-----DDYENAYKNLGEVIKEIKR-RIERLEKFIKRTENIEELIKEKEKELEE 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 625 NEKKMKEANESRLRLKRELEQARQarvcdkgcEAGRLRaKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVV 704
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEK--------EVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275


                 ....*.
gi 530360372 705 KELQEQ 710
Cdd:PRK03918 276 EELEEK 281
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 542-730 2.76e-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: 41.03  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  542 AELEHLRQALEGGL-----DTKEAKEKFLHEVVKMRVKQEEkLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRK 616
Cdd:pfam07888  44 AELLQAQEAANRQRekekeRYKRDREQWERQRRELESRVAE-LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  617 EierlRAENEKKMKEANE--SRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRER 694
Cdd:pfam07888 123 Q----RAAHEARIRELEEdiKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 530360372  695 EAREHLEKVVKELQEQLWPRARPEAAGSEGAAELEP 730
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 595-711 2.79e-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: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  595 FLRVA--KKEKLREATEAKRNLRKEIERLRAENE------KKMKEANESRLRLKRELEQARQ--ARVCdkgcEAGRLRAK 664
Cdd:COG3096   273 YMRHAneRRELSERALELRRELFGARRQLAEEQYrlvemaRELEELSARESDLEQDYQAASDhlNLVQ----TALRQQEK 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530360372  665 ---YSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:COG3096   349 ierYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 540-711 2.80e-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: 41.10  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEA----KRNLR 615
Cdd:COG5185  341 LTAEIEQGQESLTENLEAIKEEIENIVGEVELS-KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATledtLKAAD 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 616 KEIERLRAENEKKMKEaNESRLRLKRELEQARQARVCD-KGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLlreR 694
Cdd:COG5185  420 RQIEELQRQIEQATSS-NEEVSKLLNELISELNKVMREaDEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV---S 495

                        170
                 ....*....|....*..
gi 530360372 695 EAREHLEKVVKELQEQL 711
Cdd:COG5185  496 TLKATLEKLRAKLERQL 512
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
540-709 3.54e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKeakekflhevvkmrvkQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 619
Cdd:COG3206  238 AEARLAALRAQLGSGPDAL----------------PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEkkmKEANESRLRLKRELEQARQArvcdkgceagrlRAKYSAQIEDLQVKLQHAEADREQLRaDLLRERE-ARE 698
Cdd:COG3206  302 ALRAQLQ---QEAQRILASLEAELEALQAR------------EASLQAQLAQLEARLAELPELEAELR-RLEREVEvARE 365

                        170
                 ....*....|.
gi 530360372 699 HLEKVVKELQE 709
Cdd:COG3206  366 LYESLLQRLEE 376
PTZ00121 PTZ00121
MAEBL; Provisional
 576-710 3.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  576 EEKLSAALQAKRSlhqelEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANES----RLRLKRELEQARQARV 651
Cdd:PTZ00121 1094 EEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAedakRVEIARKAEDARKAEE 1168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360372  652 CDKGCEAGRLRAKYSAQIEDLQVKLQHAEADReqlRADLLREREAREHLEKVVKELQEQ 710
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDAR---KAEAARKAEEERKAEEARKAEDAK 1224
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 543-711 4.02e-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: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   543 ELEHLRQALEGglDTKEAKEKF------LHEVVKMRVKQEEKLSAAL------QAKRSL----HQELEFLRVAKKEKLR- 605
Cdd:pfam01576  205 ELEKAKRKLEG--ESTDLQEQIaelqaqIAELRAQLAKKEEELQAALarleeeTAQKNNalkkIRELEAQISELQEDLEs 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   606 ------EATEAKRNLRKEIERLRAENEKKMKE-ANESRLRLKRELEQARQARVCD---KGCEA--GRLRAKYSAQIEDLQ 673
Cdd:pfam01576  283 eraarnKAEKQRRDLGEELEALKTELEDTLDTtAAQQELRSKREQEVTELKKALEeetRSHEAqlQEMRQKHTQALEELT 362

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 530360372   674 VKLQHAEADREQLradllreREAREHLEKVVKELQEQL 711
Cdd:pfam01576  363 EQLEQAKRNKANL-------EKAKQALESENAELQAEL 393
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 540-715 4.15e-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: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKL--------------- 604
Cdd:pfam12128  324 LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiagikdklakir 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   605 ----REATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQAR--------------QARVCDKGCEAGR-LRAKY 665
Cdd:pfam12128  404 eardRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllQLENFDERIERAReEQEAA 483

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 530360372   666 SAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRA 715
Cdd:pfam12128  484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 540-686 4.26e-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: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   540 LEAELEHLRQALEGGLDT----KEAKEKFLHEVVKM-RVKQEEKLS--AALQAKRSLH-QELEFLrvakKEKLREATEAK 611
Cdd:pfam01576  297 LGEELEALKTELEDTLDTtaaqQELRSKREQEVTELkKALEEETRSheAQLQEMRQKHtQALEEL----TEQLEQAKRNK 372

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360372   612 RNLRKEIERLRAENEKKMKEAnesrlrlkRELEQARQarvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQL 686
Cdd:pfam01576  373 ANLEKAKQALESENAELQAEL--------RTLQQAKQ--------DSEHKRKKLEGQLQELQARLSESERQRAEL 431
PTZ00121 PTZ00121
MAEBL; Provisional
 557-720 4.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  557 TKEAKEKFlHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKR---NLRKEIERlRAENEKKMKEAN 633
Cdd:PTZ00121 1093 TEEAFGKA-EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKaedAKRVEIAR-KAEDARKAEEAR 1170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  634 ES----RLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADR--------EQLRADLLREREARE--H 699
Cdd:PTZ00121 1171 KAedakKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaeavkkaEEAKKDAEEAKKAEEerN 1250

                         170       180
                  ....*....|....*....|.
gi 530360372  700 LEKVVKELQEQLWPRARPEAA 720
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAA 1271
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
540-709 4.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQA--LEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKE---KLREATEAKRNL 614
Cdd:PRK02224 494 VEERLERAEDLveAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREE 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 615 RKEIERLRAENEKKM---------------KEANESRLRLKR----ELEQARQARVCDKGCEAGRLRAKY-SAQIEDLQV 674
Cdd:PRK02224 574 VAELNSKLAELKERIeslerirtllaaiadAEDEIERLREKRealaELNDERRERLAEKRERKRELEAEFdEARIEEARE 653

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530360372 675 KLQHAEADREQLRADLLREREAREHLEK----VVKELQE 709
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLQAeigaVENELEE 692
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 576-711 5.11e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 576 EEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKrelEQARQARVcdKG 655
Cdd:COG3883   29 QAELEAAQAELDALQAELE----ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---ERARALYR--SG 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360372 656 CEAGRL--------------RAKYSAQIEDLQVK-LQHAEADREQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:COG3883  100 GSVSYLdvllgsesfsdfldRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 540-711 5.45e-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: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  540 LEAELEHLRQALEGG---LDTKEAKEKFLHEVVKmrvKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRK 616
Cdd:TIGR04523 473 LSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKK---ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  617 EIERLRAENEKK-----------MKEANESRLRLKRELEQarqaRVCDKGCEAGRLR---AKYSAQIEDLQVKLQHAEAD 682
Cdd:TIGR04523 550 DDFELKKENLEKeideknkeieeLKQTQKSLKKKQEEKQE----LIDQKEKEKKDLIkeiEEKEKKISSLEKELEKAKKE 625

                         170       180
                  ....*....|....*....|....*....
gi 530360372  683 REQLRADLLREREAREHLEKVVKELQEQL 711
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 539-709 5.49e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 539 GLEAELEHLRQALE------GGLDTKEAKEKfLHEVvkmrvkQEE--KLSAALQ----AKRSLHQELEFLrvakKEKLRE 606
Cdd:PRK04778 253 DIEKEIQDLKEQIDenlallEELDLDEAEEK-NEEI------QERidQLYDILErevkARKYVEKNSDTL----PDFLEH 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 607 ATEAKRNLRKEIERLR-----AENEKkmkeanESRLRLKRELEQAR-QARVCDKGCEAGRLRakYS---AQIEDLQVKLQ 677
Cdd:PRK04778 322 AKEQNKELKEEIDRVKqsytlNESEL------ESVRQLEKQLESLEkQYDEITERIAEQEIA--YSelqEELEEILKQLE 393

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530360372 678 HAEADREQLRADL--LR--EREAREHLEKVVKELQE 709
Cdd:PRK04778 394 EIEKEQEKLSEMLqgLRkdELEAREKLERYRNKLHE 429
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 541-709 5.66e-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: 40.42  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   541 EAELEHLRQALEGgLDTKEAKEKflhevvkMRVKQEEKLSAALQAKRSLHQELEfLRVAKKEKLREATEakrNLRKEIER 620
Cdd:TIGR00606  743 EKEIPELRNKLQK-VNRDIQRLK-------NDIEEQETLLGTIMPEEESAKVCL-TDVTIMERFQMELK---DVERKIAQ 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   621 LRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHL 700
Cdd:TIGR00606  811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890


                   ....*....
gi 530360372   701 EKVVKELQE 709
Cdd:TIGR00606  891 VELSTEVQS 899
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
540-691 6.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFL--HEVVKMRVKQEEKLSAALQAKRSL---HQELEFLRVAKKEKLREATEAKRNL 614
Cdd:COG4717  100 LEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEEL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 615 RKEIERLRAENEKKMKEANES-------RLRLKRELEQARQarvcdkgcEAGRLRakysAQIEDLQVKLQHAEADREQLR 687
Cdd:COG4717  180 EELLEQLSLATEEELQDLAEEleelqqrLAELEEELEEAQE--------ELEELE----EELEQLENELEAAALEERLKE 247


                 ....
gi 530360372 688 ADLL 691
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 ...
 601-710 6.23e-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: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 601 KEKLREATEAKRNLRKEIERLRAENEKKMKEANESRlrlKRELEQARQarvcdkgcEAGRLRAKYSAQIEdlqvklqhAE 680
Cdd:cd06503   32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEA---QEIIEEARK--------EAEKIKEEILAEAK--------EE 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 530360372 681 ADR--EQLRADLLRERearehlEKVVKELQEQ 710
Cdd:cd06503   93 AERilEQAKAEIEQEK------EKALAELRKE 118
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
547-711 6.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 547 LRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAK--KEKLREATEAKRNLRkeIERLRAE 624
Cdd:COG4717  294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEelQELLREAEELEEELQ--LEELEQE 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 625 NEKKMKEAN-ESRLRLKRELEQARQARvcdkgcEAGRLRAKYSAQIEDL--QVKLQHAEADREQLRADLLREREAREHLE 701
Cdd:COG4717  372 IAALLAEAGvEDEEELRAALEQAEEYQ------ELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELE 445

                        170
                 ....*....|
gi 530360372 702 KVVKELQEQL 711
Cdd:COG4717  446 EELEELREEL 455
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 558-703 6.40e-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: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 558 KEAKEKFLhEVVKMRVKQEEKLSA-ALQAKRSLHQ----------ELEFLRVAKKEKLreATEAKRNLRKEIERLRAENE 626
Cdd:cd22656  113 EEAKKTIK-ALLDDLLKEAKKYQDkAAKVVDKLTDfenqtekdqtALETLEKALKDLL--TDEGGAIARKEIKDLQKELE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 627 KKMKEANEsrlRLKRELEQARqarvcdkgceagrlrakysAQIEDLQVKLQHAEADREQLRA------DLLRE-REAREH 699
Cdd:cd22656  190 KLNEEYAA---KLKAKIDELK-------------------ALIADDEAKLAAALRLIADLTAadtdldNLLALiGPAIPA 247


                 ....
gi 530360372 700 LEKV 703
Cdd:cd22656  248 LEKL 251
PTZ00121 PTZ00121
MAEBL; Provisional
 541-705 6.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  541 EAELEHLRQALEGGLDTKEAKEKFLHEVVK----MRVKQEEKLSAAlQAKRSLHQELEflrvaKKEKLREATEAKRN--- 613
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKAD-EAKKKAEEDKK-----KADELKKAAAAKKKade 1422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  614 LRKEIERLRAENEKKmKEANESRL--RLKRELEQARQARVCDKGCEAGR------LRAKYSAQIEDLQVKLQHAEADREQ 685
Cdd:PTZ00121 1423 AKKKAEEKKKADEAK-KKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKkadeakKKAEEAKKADEAKKKAEEAKKKADE 1501

                         170       180
                  ....*....|....*....|....*...
gi 530360372  686 LR--------ADLLREREAREHLEKVVK 705
Cdd:PTZ00121 1502 AKkaaeakkkADEAKKAEEAKKADEAKK 1529
mukB PRK04863
chromosome partition protein MukB;
541-697 6.67e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  541 EAELEHLRQA---LEGGLDTKEAKEKFLHEVV---KMRVKQEEKL--SAALQAKRSLHQELEFLRvakkEKLREATEAKR 612
Cdd:PRK04863  836 EAELRQLNRRrveLERALADHESQEQQQRSQLeqaKEGLSALNRLlpRLNLLADETLADRVEEIR----EQLDEAEEAKR 911

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  613 NLRK------EIER----LRAENE-----KKMKEANESRLRL----KRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQ 673
Cdd:PRK04863  912 FVQQhgnalaQLEPivsvLQSDPEqfeqlKQDYQQAQQTQRDakqqAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLR 991

                         170       180
                  ....*....|....*....|....
gi 530360372  674 VKLQHAEADREQLRaDLLREREAR 697
Cdd:PRK04863  992 QRLEQAEQERTRAR-EQLRQAQAQ 1014
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 599-707 7.99e-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: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 599 AKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLkreLEQARQarvcdkgcEAGRLRAKYSAQIEdlqvklQH 678
Cdd:COG0711   31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEI---IAEARK--------EAEAIAEEAKAEAE------AE 93

                         90       100       110
                 ....*....|....*....|....*....|
gi 530360372 679 AEADREQLRADLLRERE-AREHLEKVVKEL 707
Cdd:COG0711   94 AERIIAQAEAEIEQERAkALAELRAEVADL 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-707 8.39e-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: 8.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEflrvAKKEKLREATEAKRNLRKEIE 619
Cdd:COG1196  670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE----ALEEQLEAEREELLEELLEEE 745

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEANESRLRLKRELEQARQARvcdkgcEA-GR--LRAkysaqIEDLQ-VKLQHAEADREqlRADLlreRE 695
Cdd:COG1196  746 ELLEEEALEELPEPPDLEELERELERLEREI------EAlGPvnLLA-----IEEYEeLEERYDFLSEQ--REDL---EE 809

                        170
                 ....*....|..
gi 530360372 696 AREHLEKVVKEL 707
Cdd:COG1196  810 ARETLEEAIEEI 821
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 614-708 8.62e-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: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  614 LRKEIERLRAENEK----------KMKEANESRLRLKREL-----EQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQH 678
Cdd:pfam15294 131 LHMEIERLKEENEKlkerlktlesQATQALDEKSKLEKALkdlqkEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210

                          90       100       110
                  ....*....|....*....|....*....|....
gi 530360372  679 AEADREQLRADLLRER----EAREHLEKVVKELQ 708
Cdd:pfam15294 211 STALQKSLEEDLASTKhellKVQEQLEMAEKELE 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 540-711 8.76e-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: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 540 LEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIE 619
Cdd:COG1196  611 ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372 620 RLRAENEKKMKEANESRLRLKRELE-QARQARvcdkgcEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLRErEARE 698
Cdd:COG1196  691 EELELEEALLAEEEEERELAEAEEErLEEELE------EEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLE 763

                        170
                 ....*....|...
gi 530360372 699 HLEKVVKELQEQL 711
Cdd:COG1196  764 ELERELERLEREI 776
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
602-712 9.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  602 EKLREATEAKRNLRKEIERLRaenekKMKEANESRLRLKRELEQARQARvcdkgcEAGRLRAKySAQIEDLQVKLQHAEA 681
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE-----PIRELAERYAAARERLAELEYLR------AALRLWFA-QRRLELLEAELEELRA 302

                          90       100       110
                  ....*....|....*....|....*....|.
gi 530360372  682 DREQLRADLLREREAREHLEKVVKELQEQLW 712
Cdd:COG4913   303 ELARLEAELERLEARLDALREELDELEAQIR 333
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 577-627 9.47e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.05  E-value: 9.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530360372 577 EKLSAALQAKRSLHQELEFLRvakkEKLREATEAKRNLRKEIERLRAENEK 627
Cdd:PRK03992   1 ERLEALEERNSELEEQIRQLE----LKLRDLEAENEKLERELERLKSELEK 47
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 542-727 9.48e-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: 39.39  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   542 AELEHLRQALEggldtKEAKEkfLHEVVK--MRVKQE-----EKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNL 614
Cdd:pfam01576  373 ANLEKAKQALE-----SENAE--LQAELRtlQQAKQDsehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESV 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372   615 RKEIERLRAENEKKMKEAN--ESRLRLKRELEQarqarvcdkgcEAGRLRAKYSAQIEDLqvklqhaEADREQLRADLLR 692
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSslESQLQDTQELLQ-----------EETRQKLNLSTRLRQL-------EDERNSLQEQLEE 507

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 530360372   693 EREAREHLEKVVKELQEQL--WPRARPEAAGSEGAAE 727
Cdd:pfam01576  508 EEEAKRNVERQLSTLQAQLsdMKKKLEEDAGTLEALE 544
PTZ00121 PTZ00121
MAEBL; Provisional
 545-710 9.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  545 EHLRQALEGgldtKEAKEKFLHEVVKmRVKQEEKLSAALQAK--RSLHQELEFLRVAKKEKLREATEAKR--------NL 614
Cdd:PTZ00121 1137 EDARKAEEA----RKAEDAKRVEIAR-KAEDARKAEEARKAEdaKKAEAARKAEEVRKAEELRKAEDARKaeaarkaeEE 1211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360372  615 RKEIERLRAENEKKMKEANESRlRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADR--------EQL 686
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKadelkkaeEKK 1290

                         170       180
                  ....*....|....*....|....
gi 530360372  687 RADLLREREAREHLEKVVKELQEQ 710
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