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Conserved domains on  [gi|568952894|ref|XP_006508675|]
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liprin-alpha-1 isoform X26 [Mus musculus]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

liprin-alpha belongs to the LAR (leukocyte common antigen-related) family or transmembrane protein-tyrosine phosphatase-interacting proteins and is involved in formation of the presynaptic active zone

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 992-1057 4.21e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 4.21e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  992 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1057
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 884-954 1.02e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.02  E-value: 1.02e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  884 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 954
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1077-1148 2.50e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.50e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1077 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.20e-17

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196   213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         250
                  ....*....|....*....
gi 568952894  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196   449 EEEAELEEEEEALLELLAE 467
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 8.71e-13

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: 73.17  E-value: 8.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 389-660 4.68e-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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 568952894   620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 992-1057 4.21e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 4.21e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  992 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1057
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 884-954 1.02e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.02  E-value: 1.02e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  884 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 954
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1077-1148 2.50e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.50e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1077 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.20e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196   213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         250
                  ....*....|....*....
gi 568952894  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196   449 EEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 246-516 2.53e-15

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: 81.64  E-value: 2.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   397 RVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAAL 472
Cdd:TIGR02168  352 ELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKL 430

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 568952894   473 E--DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  431 EeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 991-1055 5.14e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 5.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894   991 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 8.71e-13

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: 73.17  E-value: 8.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-514 1.64e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.91  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224  309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAEL-- 394
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVeg 463

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------LHLK 466
Cdd:PRK02224  464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraEELR 543

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568952894  467 ERMAALEDKNSLLREVenAKKQLEETQhDKDQLVVTIEALKAELEQMR 514
Cdd:PRK02224  544 ERAAELEAEAEEKREA--AAEAEEEAE-EAREEVAELNSKLAELKERI 588
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-511 7.52e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 66.68  E-value: 7.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921  132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921  212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE------- 405
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltearte 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   406 -----ERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER------------- 460
Cdd:pfam15921  365 rdqfsQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallka 437

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568952894   461 ----LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:pfam15921  438 mkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-468 2.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717   167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717   233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717   308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  353 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 424
Cdd:COG4717   388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 568952894  425 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 468
Cdd:COG4717   467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1078-1148 1.36e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894   1078 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 884-950 3.39e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.39e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894    884 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 950
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1000-1055 3.49e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.49e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894   1000 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-438 9.51e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 49.68  E-value: 9.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220    5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220   85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV--IDRQ 261
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQ 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   262 AREQSQMKERLASLSSHAAE---LEEDLDTARKDLIKSEEMNTklqrevrEAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam19220  223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   339 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 418
Cdd:pfam19220  296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 568952894   419 E-------AQLEEKNQELQRARQREKM 438
Cdd:pfam19220  359 TkrfeverAALEQANRRLKEELQRERA 385
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1078-1148 4.36e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.64  E-value: 4.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  1078 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 323-444 1.32e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.96  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  323 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 389
Cdd:cd07680    61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894  390 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 444
Cdd:cd07680   141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 886-948 1.65e-03

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   886 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 948
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 389-660 4.68e-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: 41.21  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 568952894   620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 992-1057 4.21e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 150.70  E-value: 4.21e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  992 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1057
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 884-954 1.02e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.02  E-value: 1.02e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  884 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 954
Cdd:cd09562     1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1077-1148 2.50e-42

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 148.62  E-value: 2.50e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1077 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 996-1055 5.02e-29

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 110.32  E-value: 5.02e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  996 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 891-949 1.31e-26

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 103.46  E-value: 1.31e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894  891 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 949
Cdd:cd09494     1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1085-1146 2.55e-24

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 97.23  E-value: 2.55e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1085 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1146
Cdd:cd09496     1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1077-1148 7.05e-22

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 90.58  E-value: 7.05e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1077 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-512 7.20e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 RQARE-QSQMKERLASLSSHA-AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG1196   213 ERYRElKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  338 VHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         250
                  ....*....|....*....
gi 568952894  494 HDKDQLVVTIEALKAELEQ 512
Cdd:COG1196   449 EEEAELEEEEEALLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-517 8.47e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  248 LAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKR 327
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  328 YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT----LRKAETLPEVEAELAQRVAALSK 403
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  404 AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLR 480
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEeeaLEEAAEEEAELEEEEEALLELLAELLE 470

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568952894  481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 885-949 2.07e-16

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 74.80  E-value: 2.07e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894  885 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 949
Cdd:cd09564     2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1077-1148 1.22e-15

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.87  E-value: 1.22e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1077 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 246-516 2.53e-15

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: 81.64  E-value: 2.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQ-EVIDRQAREQSQMKE--------RLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEKAERYKElkaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 396
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   397 RVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAAL 472
Cdd:TIGR02168  352 ELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKL 430

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 568952894   473 E--DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  431 EeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 991-1055 2.88e-15

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 71.29  E-value: 2.88e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894  991 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 991-1055 3.23e-15

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 71.19  E-value: 3.23e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894  991 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 192-516 1.98e-14

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: 78.57  E-value: 1.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   192 LEEELGATHKELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIdrqAREQSQMKER 271
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQ---ELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE-----VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQL---E 423
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----------ELEEELEELEAALRDLESRLGDLKKERDELEAQLrelE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   424 EKNQELQRARQREKMN-----------EEHNKRLSDTVDKLLSESNERLQLH-LKERMAALEDKNSLLREVEN-AKKQLE 490
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRlselkaklealEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMlAIQEYE 982

                          330       340
                   ....*....|....*....|....*.
gi 568952894   491 ETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02169  983 EVLKRLDELKEKRAKLEEERKAILER 1008
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-516 4.15e-14

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: 77.40  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   333 REATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTlrkAETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:TIGR02168  761 AEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   413 ERLRQMEAQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260
                   ....*....|....*....|....*
gi 568952894   492 TQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELR 930
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 245-474 1.08e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  245 HEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  325 EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  405 EErhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALED 474
Cdd:COG1196   444 LE-----EAAEEEAELEEEEEALLELLAELLEEAALLEAALA----ELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 192-464 4.35e-13

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: 74.32  E-value: 4.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   192 LEEELGATHKELMI--LKEQNNQKKTLTDGLLDGNHEQESApsTNGKRSSDGSLS------HEDLAKVLELQEVIDRQAR 263
Cdd:TIGR02168  218 LKAELRELELALLVlrLEELREELEELQEELKEAEEELEEL--TAELQELEEKLEelrlevSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   264 EQSQM-------KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT-------LEKRYL 329
Cdd:TIGR02168  296 EISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLE 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   330 AAQREATSVHDLNDKLENEIA--------NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAA 400
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIAslnneierLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEE 455

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952894   401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 464
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-516 4.57e-13

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: 74.32  E-value: 4.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   187 ERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESapstngkrssdgsLSHEDLAKVLELQEVIDRQAREQS 266
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------------QISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   267 QMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLE 346
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   347 NEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAET-LPEVEAELAQRVAALSKAEERHGNIEERLRQMEaql 422
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESeLEALLNERASLEEALALLRSELEELSEELRELE--- 907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   423 eEKNQELQRARQ--REKMNEEHNK--RLSDTVDKLLSESNERLQLHLkerMAALEDKNSLLREVENAKKQLEETQHDKDQ 498
Cdd:TIGR02168  908 -SKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENKIKE 983

                          330
                   ....*....|....*....
gi 568952894   499 L-VVTIEALkAELEQMRLR 516
Cdd:TIGR02168  984 LgPVNLAAI-EEYEELKER 1001
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 991-1055 5.14e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 5.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894   991 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-462 6.87e-13

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: 73.55  E-value: 6.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168  678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHE 226
Cdd:TIGR02168  756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   227 QESAPSTNGKRSSDGSLSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR 305
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   306 EVREAMAQKEDMEERITTLEkrylaaQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQtlrkae 385
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLE------VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE------ 983

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   386 tLPEVEAElaqrvaalskAEERHGNIEERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDKLlsesNER 460
Cdd:TIGR02168  984 -LGPVNLA----------AIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NEN 1044


                   ..
gi 568952894   461 LQ 462
Cdd:TIGR02168 1045 FQ 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-432 8.71e-13

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: 73.17  E-value: 8.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   214 ktltdglLDGNHEQESAPSTNGKRSSDgsLSHEDLA----KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTA 289
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLD--ELAEELAeleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   290 RKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQER 369
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEA 462

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   370 LELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 432
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 221-512 1.71e-12

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: 72.41  E-value: 1.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   221 LDGNHEQESAPSTNGKRSSDG--SLSHEDLAKVLELQEVIDrqareqsQMKERLASLSSHAAELEEDLDTARKDLIKSEE 298
Cdd:TIGR02169  644 LEGELFEKSGAMTGGSRAPRGgiLFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   299 MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLELAEQKLQ 378
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNDLEARLS 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   379 QtlrkaETLPEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKL 453
Cdd:TIGR02169  790 H-----SRIPEIQAE-------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKE 855

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894   454 LSESN---ERLQLHLKERMAALED----KNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:TIGR02169  856 IENLNgkkEELEEELEELEAALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-441 4.70e-12

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: 67.26  E-value: 4.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  245 HEDLAKVLELQEvIDRQAReqsQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTL 324
Cdd:COG1579     3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  325 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 404
Cdd:COG1579    79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568952894  405 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMNEE 441
Cdd:COG1579   144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-672 9.64e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 9.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  155 SSEVEVLKALKSL--FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAps 232
Cdd:COG1196   219 KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-- 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  233 tngKRSSDGSLSHEdLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMA 312
Cdd:COG1196   297 ---LARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  313 QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEA 392
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAE 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  393 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllsESNERLQLHLKERMAAL 472
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG-------FLEGVKAALLLAGLRGL 522

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  473 EDKNSLLREVENAKKQLEET----------QHDKDQLVVTIEALKAE---------LEQMRLRGPSLHHGRPHLGS---- 529
Cdd:COG1196   523 AGAVAVLIGVEAAYEAALEAalaaalqnivVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGaavd 602

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  530 ------VPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTL------------------NEQDWERAQQASV 585
Cdd:COG1196   603 lvasdlREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggsaggsltggsrreLLAALLEAEAELE 682

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  586 LANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQ---------RA 656
Cdd:COG1196   683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppDL 762

                         570
                  ....*....|....*...
gi 568952894  657 EEIESRVGS--GSLDNLG 672
Cdd:COG1196   763 EELERELERleREIEALG 780
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-514 1.64e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.91  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKR 237
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  238 SSDGSLSHEDLAKVL-ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKED 316
Cdd:PRK02224  309 AEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  317 MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAEL-- 394
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVeg 463

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------LHLK 466
Cdd:PRK02224  464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraEELR 543

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568952894  467 ERMAALEDKNSLLREVenAKKQLEETQhDKDQLVVTIEALKAELEQMR 514
Cdd:PRK02224  544 ERAAELEAEAEEKREA--AAEAEEEAE-EAREEVAELNSKLAELKERI 588
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 884-948 3.08e-11

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 59.93  E-value: 3.08e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  884 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 948
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
mukB PRK04863
chromosome partition protein MukB;
179-508 5.10e-11

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 67.67  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  179 RERLRVALERCSLLEEELGATHKELmiLKEQnnQKKTLTDGLLDGNHEQESAPSTNGKRSSDgslsHedLAKVLE---LQ 255
Cdd:PRK04863  278 ANERRVHLEEALELRRELYTSRRQL--AAEQ--YRLVEMARELAELNEAESDLEQDYQAASD----H--LNLVQTalrQQ 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  256 EVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEmntklqrEVREAMAQKEDMEERITTLEKR---YLAAQ 332
Cdd:PRK04863  348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQQTRaiqYQQAV 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------------QTLRKAetLPEVEAELAQRVA 399
Cdd:PRK04863  421 QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AGEVSRSEAWDVA 498

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  400 --ALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLKERMAALEDKNS 477
Cdd:PRK04863  499 reLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQEELEARLESLSE 572

                         330       340       350
                  ....*....|....*....|....*....|.
gi 568952894  478 llrEVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863  573 ---SVSEARERRMALRQQLEQLQARIQRLAA 600
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-511 7.52e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 66.68  E-value: 7.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVL---------------ELQEVIDRQAREQSQMK 269
Cdd:pfam15921  132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilvDFEEASGKKIYEHDSMS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   270 E-RLASLSSHAAELEEDLDTARKDLI--------KSEEMNTKLQREVREAMAQKEDMEER--------ITTLEKRYLAAQ 332
Cdd:pfam15921  212 TmHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRIEQliseheveITGLTEKASSAR 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   333 REATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAE------- 405
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEltearte 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   406 -----ERHGNIEERLRQMEAQLEEKNQELQrarqrekMNEEHNKRLSD-------TVDKLLSESNER------------- 460
Cdd:pfam15921  365 rdqfsQESGNLDDQLQKLLADLHKREKELS-------LEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallka 437

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568952894   461 ----LQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:pfam15921  438 mkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-491 1.17e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  125 LEHLEcLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196   417 ERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  205 ILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEE 284
Cdd:COG1196   496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  285 DLdtaRKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEdKNR 364
Cdd:COG1196   576 FL---PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTL 651

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  365 QLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:COG1196   652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 568952894  445 RLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:COG1196   732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 44-513 1.36e-10

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 66.15  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618  417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618  497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   203 LMILKEQNNQKKTLTDGLLdgNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQ--AREQSQMKERLASLSSHAA 280
Cdd:TIGR00618  572 FSILTQCDNRSKEDIPNLQ--NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALH 649

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   281 ELEEDL------DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDlNDKLENEIANKDS 354
Cdd:TIGR00618  650 ALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE-YDREFNEIENASS 728

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   355 MHRQTedknrqLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGnieERLRQMEAQLEEKNQELQRARQ 434
Cdd:TIGR00618  729 SLGSD------LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---AELSHLAAEIQFFNRLREEDTH 799

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894   435 REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:TIGR00618  800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-660 2.27e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQ---- 227
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleel 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  228 -ESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQRE 306
Cdd:COG1196   322 eEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  307 VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTLRKAEt 386
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------EEAAEEEAELEEEEEALLELLAELLEEAA- 473

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  387 lpEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNK--RLSDTVDKLLSESNERLQLH 464
Cdd:COG1196   474 --LLEAALAELLEELAEAAAR----LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvaVLIGVEAAYEAALEAALAAA 547

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  465 LKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFsvadGHVDA 544
Cdd:COG1196   548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL----GDTLL 623

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  545 YSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:COG1196   624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 568952894  625 QTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:COG1196   704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-514 2.95e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  267 QMKERLASLSSHAAELEEDLDtarkdlikseemntKLQREVREAmAQKEDMEERITTLEKRYLAAQREAtsVHDLNDKLE 346
Cdd:COG1196   183 ATEENLERLEDILGELERQLE--------------PLERQAEKA-ERYRELKEELKELEAELLLLKLRE--LEAELEELE 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  347 NEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHgniEERLRQMEAQLEEKN 426
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELE 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  427 QELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDK 496
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAeeeleeaeaeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         250
                  ....*....|....*...
gi 568952894  497 DQLVVTIEALKAELEQMR 514
Cdd:COG1196   403 EELEEAEEALLERLERLE 420
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 272-519 4.26e-10

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: 63.24  E-value: 4.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  272 LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlaaqreatsvhdlnDKLENEIAN 351
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  352 KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETL---PEVEAELAQR-VAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  428 ELQRARQREkmnEEHNKRLSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:COG4942   161 ELAALRAEL---EAERAELEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLE 233

                         250
                  ....*....|..
gi 568952894  508 AELEQMRLRGPS 519
Cdd:COG4942   234 AEAAAAAERTPA 245
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-516 4.41e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 64.31  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlndkleNEIankdsmhrqtEDKN 363
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-----------NEI----------SSEL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMNE 440
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYI 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  441 EHNKRLSDTVDKL------LSESNERLQlHLKERMAALEDKNSLLREVENAKKQLE---ETQHDKDQLVVTIEALKAELE 511
Cdd:PRK03918  297 KLSEFYEEYLDELreiekrLSRLEEEIN-GIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELE 375


                  ....*
gi 568952894  512 QMRLR 516
Cdd:PRK03918  376 RLKKR 380
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 246-511 5.20e-10

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: 64.32  E-value: 5.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNtKLQREVREA-----MAQKEDMEER 320
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQ 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   321 ITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERLELAEQKLQQTLRkaETLPEVEAELAQRVAA 400
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERS 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   401 LSKAEERHGNIEERLRQMEAQLEEKNQEL--------QRARQREKMNEEHnKRLSDTVDKLLSE------SNERLQLHLK 466
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLAEIeelereieEERKRRDKLTEEY-AELKEELEDLRAEleevdkEFAETRDELK 388

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568952894   467 ERMAALED----KNSLLREVE---NAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR02169  389 DYREKLEKlkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINELE 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-491 6.58e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLtDGLLDGNHEQESAP 231
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFY 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  232 STNGKRSSDGSlshEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR----EV 307
Cdd:PRK03918  303 EEYLDELREIE---KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKK 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  308 REAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AE 385
Cdd:PRK03918  380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKGKCPVCGRELTEEHRKELLEEyTA 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  386 TLPEVEAELAQRVAALSKAEERHGNIEE---------RLRQMEAQLEEKNQELqrarqrEKMNEEHNKRLSDTVDKLLSE 456
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKL------KKYNLEELEKKAEEYEKLKEK 533

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568952894  457 SN--ERLQLHLKERMAALEDKNSLLREVENAKKQLEE 491
Cdd:PRK03918  534 LIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
PTZ00121 PTZ00121
MAEBL; Provisional
 236-498 8.05e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  236 KRSSDGSLSHEDLAKVLELQEVID--RQAREQSQMKE-RLASLSSHAAELEEDLDTARKD-LIKSEEMntKLQREVREAM 311
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKADeLKKAEEL--KKAEEKKKAE 1567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  312 AQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERLELAEQKLQQTLR 382
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKK 1647

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesnERLQ 462
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELK 1722

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568952894  463 LHLKERMAALEDknsLLREVENAKKQLEETQHDKDQ 498
Cdd:PTZ00121 1723 KAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-512 1.57e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   110 EIAELKAErnntrlllehleclvsrherslrmtvVKRQAqspagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALErc 189
Cdd:TIGR02168  678 EIEELEEK--------------------------IEELE------EKIAELEKALAELRKELEELEEELEQLRKELEE-- 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   190 slLEEELGATHKELMIL-KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQM 268
Cdd:TIGR02168  724 --LSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 348
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   349 IAnkdsmhrqtedknrQLQERLELAEQKLQQtlrKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKnqe 428
Cdd:TIGR02168  882 RA--------------SLEEALALLRSELEE---LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--- 941

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   429 LQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKER-------MAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

                          410
                   ....*....|.
gi 568952894   502 TIEALKAELEQ 512
Cdd:TIGR02168 1022 AIEEIDREARE 1032
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 38-529 1.66e-09

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: 62.37  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606  353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606  433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   189 CSLLEEElgatHKELMILKEQNNQKKTLTDGLL---DGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ 265
Cdd:TIGR00606  511 ADLDRKL----RKLDQEMEQLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   266 SQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 342
Cdd:TIGR00606  587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELA----QRVAALSKAEERHGNIEERLRQ 417
Cdd:TIGR00606  666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIIDLKEKE 745

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   418 MEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREV 482
Cdd:TIGR00606  746 IP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTV 824

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 568952894   483 ENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGS 529
Cdd:TIGR00606  825 QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
254-520 3.63e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  254 LQEVIdrqaREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRylaaQR 333
Cdd:PRK03918  167 LGEVI----KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK03918  239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLLrEVENAKKQ 488
Cdd:PRK03918  319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL-TPEKLEKE 392

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568952894  489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSL 520
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKEL 424
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 249-516 4.70e-09

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 60.08  E-value: 4.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:pfam19220   48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   329 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:pfam19220  128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   409 gniEERLRQMEAQLEEKNQELQRA-RQREKMNEEHNKRLSdTVDKLLSESNERL----QLhLKERMAALEDKNSLLREVE 483
Cdd:pfam19220  208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERA-SLRMKLEALTARAaateQL-LAEARNQLRDRDEAIRAAE 282

                          250       260       270
                   ....*....|....*....|....*....|...
gi 568952894   484 NAkkqLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam19220  283 RR---LKEASIERDTLERRLAGLEADLERRTQQ 312
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 258-441 5.35e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.84  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREV----REAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  334 ------------EATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEAEL 394
Cdd:COG3883    98 sggsvsyldvllGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQ 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568952894  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-435 7.38e-09

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: 59.39  E-value: 7.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYlAAQ 332
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-AEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  333 REATSVHDLNDKLENEIANKD------------SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA 400
Cdd:COG4942   110 LRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568952894  401 LSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4942   190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-452 8.28e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 8.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  197 GATHKELmiLKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG1196   559 AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  277 SHAAELEEDLDTARKDL-----------IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL 345
Cdd:COG1196   637 RRAVTLAGRLREVTLEGeggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  346 ENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EER 414
Cdd:COG1196   717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEER 796

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 568952894  415 LRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 452
Cdd:COG1196   797 YDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 302-493 8.30e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.07  E-value: 8.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTL 381
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  382 RKAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL 453
Cdd:COG3883    97 RSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568952894  454 LSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-441 1.03e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKELnvcreqlleREEEIAELKAERNNTRLL 124
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEK---------REYEGYELLKEKEALERQ 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   125 LEHLECLVSRHERSLRmtvvKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRValercsllEEELGATHKELM 204
Cdd:TIGR02169  239 KEAIERQLASLEEELE----KLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRV--------KEKIGELEAEIA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   205 ILKEQNNQKKtltdglldgnHEQESApstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAslsshaaELEE 284
Cdd:TIGR02169  305 SLERSIAEKE----------RELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894   365 QLQERLELAEQKLQQTlrkaetlpeveaelaqrVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 441
Cdd:TIGR02169  445 DKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 315-582 1.16e-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: 59.69  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   315 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ-TLRKAETLPEVEAE 393
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   394 LAQRVAALSKAEErhgnieerLRQMEAQLEEKNQELQraRQREKMNEEHNkrlsdTVDKLLSESNERLQLHLKERMAALE 473
Cdd:TIGR02168  760 EAEIEELEERLEE--------AEEELAEAEAEIEELE--AQIEQLKEELK-----ALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRR 553
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          250       260       270
                   ....*....|....*....|....*....|..
gi 568952894   554 PQKGRLAALRDEPSKVQTLNEQ---DWERAQQ 582
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQlelRLEGLEV 936
PRK12704 PRK12704
phosphodiesterase; Provisional
 360-511 1.39e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 59.02  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  360 EDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 439
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568952894  440 EEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIEAlKAELE 511
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIEE-EAKEE 185
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-514 1.70e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.98  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    31 DADSHFEQLMVSMLEERDrlldTLRETQETLALTQGKLHEVGHERDSLQ----RQLNTALPQEFAALTKELNVCREQLLE 106
Cdd:pfam15921  167 DSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFP 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   107 REEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MTVVKRQAQSPA-GVSSEVEV------------LKALKSL 167
Cdd:pfam15921  243 VEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLTEKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDL 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   168 FEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQ----KKTLTD---GLLDGNHEQESAPSTNGK---- 236
Cdd:pfam15921  323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqeSGNLDDqlqKLLADLHKREKELSLEKEqnkr 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   237 ---RSSDGSLSHEDLAKVL-------------------ELQEVIDRQAREQSQMKERLASLSSHAAELE----------E 284
Cdd:pfam15921  403 lwdRDTGNSITIDHLRRELddrnmevqrleallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvE 482

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   285 DLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15921  483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   365 Q---LQERLELAEQKLQQTLRKAETL----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEknQELQRArqreK 437
Cdd:pfam15921  563 VieiLRQQIENMTQLVGQHGRTAGAMqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD--LELEKV----K 636

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   438 MNEEHNKRLSDTVDKllseSNERLQLhLKERMAALEDKNSLLREVE----NAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam15921  637 LVNAGSERLRAVKDI----KQERDQL-LNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711


                   .
gi 568952894   514 R 514
Cdd:pfam15921  712 R 712
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 156-463 2.56e-08

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: 58.21  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   156 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVA-------LERCSLLEEELGATHKEL----MILKEQNNQKkt 215
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMdrqaAIYAEQERMA-- 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   216 ltdglLDGNHEQESAPSTNGKRSSDgSLSHEDLAKVLELQEVIDRQAREQSQMKERLaslsshaaelEEDLDTARKDLIK 295
Cdd:pfam17380  344 -----MERERELERIRQEERKRELE-RIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKIL 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   296 SEEMNTKLQREVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 363
Cdd:pfam17380  408 EEERQRKIQQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   364 RQLQERLELAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREK 437
Cdd:pfam17380  488 RAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565

                          330       340
                   ....*....|....*....|....*.
gi 568952894   438 MNEEHNKRLSDTVDKLLSESNERLQL 463
Cdd:pfam17380  566 SRLEAMEREREMMRQIVESEKARAEY 591
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-468 2.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717   167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  200 HKELMILKEQNNQKKTLTDGLLDGnheqeSAPSTNGKRSSDGSLSHEDLAKVLELQEVI-------DRQAREQSQMKERL 272
Cdd:COG4717   233 ENELEAAALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGLLallflllAREKASLGKEAEEL 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  273 ASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4717   308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  353 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 424
Cdd:COG4717   388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 568952894  425 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 468
Cdd:COG4717   467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-514 3.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLqrqlnTALPQEFAALTKELNVCREQLLEREEEIAELKA 116
Cdd:PRK03918  199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSKRKLEEKIRELEERIEELKK 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagVSSEVEvlKALKSLFEHHKALDEKVRErLRVALERCSLLEEEL 196
Cdd:PRK03918  274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIE--KRLSRLEEEINGIEERIKE-LEEKEERLEELKKKL 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  197 GATHKELMILKEQN---NQKKTLTDGLldgnheqesapstNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQ-SQMKERL 272
Cdd:PRK03918  348 KELEKRLEELEERHelyEEAKAKKEEL-------------ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARI 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  273 ASLSSHAAELE---EDLDTA---------------RKDLIK--SEEMNtKLQREVREAMAQKEDMEERITTLEKrYLAAQ 332
Cdd:PRK03918  415 GELKKEIKELKkaiEELKKAkgkcpvcgrelteehRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKE 492

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  333 REATSVHDLNDKLEN-----EIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEER 407
Cdd:PRK03918  493 SELIKLKELAEQLKEleeklKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  408 HGNIEERLRQM----EAQLEEKNQELQR----------ARQREKMNEEHNKRLSDTVDKL---LSESNERLQlHLKERMA 470
Cdd:PRK03918  572 LAELLKELEELgfesVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAfeeLAETEKRLE-ELRKELE 650

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894  471 ALEDKNS-------------LLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PRK03918  651 ELEKKYSeeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 353-514 6.43e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 56.38  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  353 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL-QR 431
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  432 ARQREKmneehNKRLSDTVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:COG3883    92 ARALYR-----SGGSVSYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164


                  ....*.
gi 568952894  509 ELEQMR 514
Cdd:COG3883   165 ELEAAK 170
PRK11281 PRK11281
mechanosensitive channel MscK;
314-514 7.72e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 56.84  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 392
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  393 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLSDTVDKLLSESN--ERLQLHLKERMA 470
Cdd:PRK11281  113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568952894  471 ALEDKNSLLREVENAKKQLEETQhdKDQLVVTIEALKAELEQMR 514
Cdd:PRK11281  171 RLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQR 212
PTZ00121 PTZ00121
MAEBL; Provisional
 169-514 1.19e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDglLDGNHEQESAPSTNGKRSSDGSLSHEDL 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  249 AKVLELQEVIDrQAREQSQMKERLASLSSHAAELE--EDLDTARKDLIKSEEMNTKLQrEVREAMAQKEDMEERITTLE- 325
Cdd:PTZ00121 1424 KKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADe 1501

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  326 -KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAAL 401
Cdd:PTZ00121 1502 aKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMAL 1580

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  402 SKAEE----RHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAL 472
Cdd:PTZ00121 1581 RKAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 568952894  473 EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
331-661 1.27e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.20  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  331 AQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGN 410
Cdd:PRK02224  197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  411 IEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------LSESNERLQLH------LKERMAALED 474
Cdd:PRK02224  277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrdrLEECRVAAQAHneeaesLREDADDLEE 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  475 KNSLLRE-VENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRgpsLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRr 553
Cdd:PRK02224  357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDFLEELREERDELREREAELE- 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  554 pqkGRLAALRDEPSKVQTLNE--------QDWERAQQASVLANVAQAFES-DVDVSDGEDDRDTLLSSVDLLSPSGQADA 624
Cdd:PRK02224  433 ---ATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVEElEAELEDLEEEVEEVEERLERAEDLVEAED 509

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568952894  625 QtlAMMLQEQLDAINKeirLIQEEKENTEQRAEEIES 661
Cdd:PRK02224  510 R--IERLEERREDLEE---LIAERRETIEEKRERAEE 541
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1078-1148 1.36e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 1.36e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894   1078 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
246-435 1.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  246 EDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLdtarkdlikseemntkLQREVREAMAQKEDMEERITTLE 325
Cdd:COG4913   252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEAELEELRAELARLEAELERLE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  326 KRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQkLQQTLRKAE-TLPEVEAELAQRVAAL--- 401
Cdd:COG4913   316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRAEAaal 392

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568952894  402 --------SKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 435
Cdd:COG4913   393 lealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-509 1.57e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913   281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913   361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913   441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  218 DGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQareqsqmkerLASLSSHA-AELEEDLDTARKD---- 292
Cdd:COG4913   511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE----------LGRRFDYVcVDSPEELRRHPRAitra 580

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  293 -LIKSE----EMNTklQREVRE-------AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLEN--EIANKDSMHRQ 358
Cdd:COG4913   581 gQVKGNgtrhEKDD--RRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSW 658

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  359 TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekm 438
Cdd:COG4913   659 DEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--- 735

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  439 neehnkrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:COG4913   736 -----------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 253-513 2.07e-07

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: 55.57  E-value: 2.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREamaqkedmeerittLEKRYLAAQ 332
Cdd:pfam01576  360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE--------------LQARLSESE 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   333 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--QTLRKAETLPEVeaelaqrvaalskaeerhgN 410
Cdd:pfam01576  426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL-------------------N 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   411 IEERLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLE 490
Cdd:pfam01576  487 LSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562

                          250       260
                   ....*....|....*....|...
gi 568952894   491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576  563 EKAAAYDKLEKTKNRLQQELDDL 585
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-512 2.09e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.41  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:TIGR04523  124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   125 LEHLECLVSRHeRSLRMTVVKRQAQSpagvSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL- 203
Cdd:TIGR04523  203 LSNLKKKIQKN-KSLESQISELKKQN----NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELe 277

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   204 ---MILKEQNNQKKTLTDGLLDGNHEQEsapstngkrssdgslshEDLAKvlELQEVIDRQAREQSQMKERLASLSSHAA 280
Cdd:TIGR04523  278 qnnKKIKELEKQLNQLKSEISDLNNQKE-----------------QDWNK--ELKSELKNQEKKLEEIQNQISQNNKIIS 338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   281 ELEEDLDTARKDLIKSEEMNTKLQREVREamaqKEDMEERIttlekrylaaQREATSVHDLNDKLENEIANKDSMHRQTE 360
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQE 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   361 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN- 439
Cdd:TIGR04523  405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNl 484

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   440 EEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDKNSLL----REVENAKKQLE------ETQHDKDQLVVTIEALKAE 509
Cdd:TIGR04523  485 EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLkekiEKLESEKKEKEskisdlEDELNKDDFELKKENLEKE 562


                   ...
gi 568952894   510 LEQ 512
Cdd:TIGR04523  563 IDE 565
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-516 2.29e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGLLD-----GNHEQESA---PSTNGKRSSDGS-------LSHEDLAKVL 252
Cdd:PRK03918  375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKitariGELKKEIKelkKAIEELKKAKGKcpvcgreLTEEHRKELL 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  253 -ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK--------DLIKS--EEMNTKLQREVREAMAQKEDMEERI 321
Cdd:PRK03918  455 eEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKEleEKLKKYNLEELEKKAEEYEKLKEKL 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  322 TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQER-------LELAEQKLQQTLRKAETLPEVEAEL 394
Cdd:PRK03918  535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeLEERLKELEPFYNEYLELKDAEKEL 614

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  395 AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQreKMNEEHNKRLSDTVDKL------LSESNERLQLHLKER 468
Cdd:PRK03918  615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELsrelagLRAELEELEKRREEI 692

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568952894  469 MAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIE---ALKAELEQMRLR 516
Cdd:PRK03918  693 KKTLEKLKEELEEREKAKKELEKLEKALERVEELREkvkKYKALLKERALS 743
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
249-512 3.35e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  249 AKVLELQEVIDRqAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRy 328
Cdd:PRK02224  489 EEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE- 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  329 laAQREATSVHDLNDKLEneiANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSkaeERH 408
Cdd:PRK02224  567 --AEEAREEVAELNSKLA---ELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---ERK 636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  409 GNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNSLLREVE 483
Cdd:PRK02224  637 RELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVEALEALY 714

                         250       260
                  ....*....|....*....|....*....
gi 568952894  484 NAKKQLEETQHDkdqlvvtieaLKAELEQ 512
Cdd:PRK02224  715 DEAEELESMYGD----------LRAELRQ 733
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 884-950 3.39e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.39e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894    884 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 950
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1000-1055 3.49e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.45  E-value: 3.49e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894   1000 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-512 3.54e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  124 LLEHLECLVSRHERSLRMTVVKRQAQSPAGV-------------------SSEVEVLKALKSLFEHHKALDEKVRERLRV 184
Cdd:COG4717   117 ELEKLEKLLQLLPLYQELEALEAELAELPERleeleerleelreleeeleELEAELAELQEELEELLEQLSLATEEELQD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  185 ALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQARE 264
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  265 QSQMKERLASLSSHAAeleedldTARKDLIKSEEMNTKLQREVREAMAQKE-DMEERITTLEKRYLAAQREATSVHDLND 343
Cdd:COG4717   272 ILTIAGVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLD 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  344 KleneIANKDSMHRQTEDKNRQLQerLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEErhgnIEERLRQMEAQLE 423
Cdd:COG4717   345 R----IEELQELLREAEELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLE 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  424 EKNQELQRARQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LREVENAKKQLEETQHD 495
Cdd:COG4717   413 ELLGELEELLEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQELEELKAELRELAEE 491

                         490
                  ....*....|....*..
gi 568952894  496 KDQLVVTIEALKAELEQ 512
Cdd:COG4717   492 WAALKLALELLEEAREE 508
PTZ00121 PTZ00121
MAEBL; Provisional
 236-507 5.29e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  236 KRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE 315
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  316 DMEE--RITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:PTZ00121 1310 KAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  394 LAQRVAALSKAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEhnKRLSDTVDKLLSESN--ERLQLHLK 466
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKkaEEAKKKAE 1467

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568952894  467 ERMAA--LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:PTZ00121 1468 EAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
307-516 5.84e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  307 VREAMAQKEDMEERITTLE---KRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTL 381
Cdd:COG4913   213 VREYMLEEPDTFEAADALVehfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  382 RKAEtLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ-----------LEEKNQELQRARQREKMNEEHNKRLSDTV 450
Cdd:COG4913   293 LEAE-LEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqLEREIERLERELEERERRRARLEALLAAL 371

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894  451 DKLLSESNERLQLHLKERMAALEDKNSLLREVEN----AKKQLEETQHDKDQLVVTIEALK-------AELEQMRLR 516
Cdd:COG4913   372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLErrksnipARLLALRDA 448
PTZ00121 PTZ00121
MAEBL; Provisional
 260-663 6.58e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 RQAREQSQMKERLASLSSHAAELEEDLDTARK---DLIKSEEMNTKLQREVREAMAQKEDMEERittlEKRYLAAQREAT 336
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAE 1353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  337 SVhdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ--KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PTZ00121 1354 AA---ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  415 LRQMEAQleEKNQELQRARQREKMNEEhnKRLSDTVDKLLSEsnerlqlhlKERMAALEDKNSLLREVENAKKQLEETQH 494
Cdd:PTZ00121 1431 KKADEAK--KKAEEAKKADEAKKKAEE--AKKAEEAKKKAEE---------AKKADEAKKKAEEAKKADEAKKKAEEAKK 1497

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  495 DKDQLVVTIEAlKAELEQMRlrgpslhhgrphlgsvpdfrfsvadgHVDAYSTSAVLRRPQKGRLAalrDEPSKVQTLNE 574
Cdd:PTZ00121 1498 KADEAKKAAEA-KKKADEAK--------------------------KAEEAKKADEAKKAEEAKKA---DEAKKAEEKKK 1547

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  575 QD----WERAQQASVLANVAQAFESdvdvsdgEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKE 650
Cdd:PTZ00121 1548 ADelkkAEELKKAEEKKKAEEAKKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                         410
                  ....*....|....*
gi 568952894  651 NTEQ--RAEEIESRV 663
Cdd:PTZ00121 1621 KAEElkKAEEEKKKV 1635
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-514 6.84e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  124 LLEhleclvsrhERSLRMTVVKRQAQSPAGVSSEVEvlKALKSLFEHHKALD---EKVRERLRVALERCSLLEEELGATH 200
Cdd:PRK02224  329 RLE---------ECRVAAQAHNEEAESLREDADDLE--ERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELR 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  201 KELMILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID----RQAREQSQMKERLASLS 276
Cdd:PRK02224  398 ERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDR 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  277 SHAAELEEDLDTARKDLiksEEMNTKLQR--EVREAMAQKEDMEERITTLEKRylAAQREATsVHDLNDKLENEIANKDS 354
Cdd:PRK02224  475 ERVEELEAELEDLEEEV---EEVEERLERaeDLVEAEDRIERLEERREDLEEL--IAERRET-IEEKRERAEELRERAAE 548

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  355 MHRQTEDKNRQLQERLELAEQKLqqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARQ 434
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAR-----------EEVAELNSKLAELKERIESLERIRTLL----AAIADAEDEIERLRE 613

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  435 REK----MNEEHNKRLS---DTVDKLLSESNE-RLQlhlkermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEAL 506
Cdd:PRK02224  614 KREalaeLNDERRERLAekrERKRELEAEFDEaRIE-------EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV 686


                  ....*...
gi 568952894  507 KAELEQMR 514
Cdd:PRK02224  687 ENELEELE 694
PTZ00121 PTZ00121
MAEBL; Provisional
 145-504 7.41e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEElgatHKELMILKEQNNQKKTLTDGLLD 222
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKAE 1531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  223 GNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAE---------LEEDLDTARKD 292
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEarieevmklYEEEKKMKAEE 1611

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  293 LIKSEEMNTKLQrEVREAmaqkEDMEERITTLEKRYLAAQREATSVHDLNDklENEIANKDSMHRQTEDKNR--QLQERL 370
Cdd:PTZ00121 1612 AKKAEEAKIKAE-ELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKaeEAKKAE 1684

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtV 450
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----I 1759

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568952894  451 DKLLSESNERLQLHLKERMAALEDKnsLLREVENAKKQLEETQHD-KDQLVVTIE 504
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDiFDNFANIIE 1812
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 302-474 7.78e-07

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: 51.46  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  302 KLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTL 381
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  382 RKAETLPEVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERL 461
Cdd:COG1579    86 RNNKEYEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                         170
                  ....*....|...
gi 568952894  462 QLHLKERMAALED 474
Cdd:COG1579   159 EELEAEREELAAK 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 133-475 1.31e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   133 SRHERSLRMTVVKRQAQSPAgVSSEVEVLKALKS-----LFEHHKALDEKvRERLRVALERCSLLEEELGATHKELMILK 207
Cdd:TIGR02169  659 SRAPRGGILFSRSEPAELQR-LRERLEGLKRELSslqseLRRIENRLDEL-SQELSDASRKIGEIEKEIEQLEQEEEKLK 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   208 EQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLE------LQEVIDRQAREQSQMKERLASLSSHAAE 281
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   282 LEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREA----TSVHDLNDKLEN---EIANKDS 354
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleAALRDLESRLGDlkkERDELEA 896

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   355 MHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA----------LSKAEERHGNIEERLRQMEAQLEE 424
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPVNML 976

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568952894   425 KNQELqrarqrekmnEEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDK 475
Cdd:TIGR02169  977 AIQEY----------EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1000-1051 1.32e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 46.46  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568952894 1000 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1051
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 38-513 1.38e-06

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: 52.92  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128  231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGLLDGnheQESApstngkrssdgsLSHEDLAKVLELQEVIDRQARE 264
Cdd:pfam12128  384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESE------------LREQLEAGKLEFNEEEYRLKSR 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   265 QSQMKERLASLSSHAAELE------EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam12128  446 LGELKLRLNQATATPELLLqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   339 --------HDLNDKLENEIAN-KDS---------MHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpev 390
Cdd:pfam12128  526 elqlfpqaGTLLHFLRKEAPDwEQSigkvispelLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL--- 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK---E 467
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanE 682

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568952894   468 RMAALE-DKNSLLREVENAKKQ-----LEETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam12128  683 RLNSLEaQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQLALL 734
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-513 1.41e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  160 VLKALKSLFEhhKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESApstnGKRSS 239
Cdd:COG4717    39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  240 DGSLSHEDLAKVLELQEVIDRQAREQSQMK---ERLASLSSHAA---ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ 313
Cdd:COG4717   113 ELREELEKLEKLLQLLPLYQELEALEAELAelpERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEE 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  314 K-EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA------------------- 373
Cdd:COG4717   193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsli 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  374 ------------------------EQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIE-----------ERLRQM 418
Cdd:COG4717   273 ltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldriEELQEL 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  419 EAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL----------------LSESNERLQLHLKERMAALE--DKNSLLR 480
Cdd:COG4717   353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELraaleqaeeyqelkeeLEELEEQLEELLGELEELLEalDEEELEE 432

                         410       420       430
                  ....*....|....*....|....*....|...
gi 568952894  481 EVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG4717   433 ELEELEEELEELEEELEELREELAELEAELEQL 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 269-511 1.92e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   269 KERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEK-------RYLAAQREATSVHDL 341
Cdd:TIGR04523   95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   342 NDKLENEIANKDSMHRQTEDKNRQLQERL---------------ELAEQKLQQTLRKaETLPEVEAELAQRVAALSKAEE 406
Cdd:TIGR04523  175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknkslesQISELKKQNNQLK-DNIEKKQQEINEKTTEISNTQT 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   407 RHGNIEERLRQMEAQLEEKNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENak 486
Cdd:TIGR04523  254 QLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN-- 328

                          250       260
                   ....*....|....*....|....*
gi 568952894   487 kQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523  329 -QISQNNKIISQLNEQISQLKKELT 352
PTZ00121 PTZ00121
MAEBL; Provisional
 246-509 2.09e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  246 EDLAKVLELQEVID-RQAREQSQMKERLASLSSHAAELEEDLDTARK-DLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:PTZ00121 1185 EEVRKAEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  324 LEKRYLAAQ----REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQE--RLELAEQKLQQTLRKAETLPEvEAELAQR 397
Cdd:PTZ00121 1265 FARRQAAIKaeeaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-KAEEAKK 1343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  398 VAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQlHLKERMAA------ 471
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAkkkade 1422

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568952894  472 LEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAE 509
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 224-498 4.23e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 50.19  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   224 NHEQESAPSTNGKRSSDGSL------SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSE 297
Cdd:pfam15905   42 NNSKDASTPATARKVKSLELkkksqkNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLS 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   298 EMNTKLQREVREAMAQKEDMEE-----------RITTLEKRYLAAQREAT--SVHDLNDKLENEIANKDSMHRQTEDKNR 364
Cdd:pfam15905  122 ASVASLEKQLLELTRVNELLKAkfsedgtqkkmSSLSMELMKLRNKLEAKmkEVMAKQEGMEGKLQVTQKNLEHSKGKVA 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   365 QLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNK 444
Cdd:pfam15905  202 QLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894   445 RLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVENAKKQL--EETQHDKDQ 498
Cdd:pfam15905  275 KQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 129-515 4.98e-06

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: 50.66  E-value: 4.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   129 ECLVSRHErslrmtVVKRQAQSPAGVSSEVEVLKALKSLFEH-HKALDEKVrERLRVALERCSLLEEELGATHKELMILK 207
Cdd:pfam07888   38 ECLQERAE------LLQAQEAANRQREKEKERYKRDREQWERqRRELESRV-AELKEELRQSREKHEELEEKYKELSASS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   208 EQNNQKKtltDGLLDGNHEQEsapstngkrssdgslshedlAKVLELQEVIdRQAREQSQMKErlaslsshaAELEEDLD 287
Cdd:pfam07888  111 EELSEEK---DALLAQRAAHE--------------------ARIRELEEDI-KTLTQRVLERE---------TELERMKE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   288 TARKDLIKSEE-------MNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLeNEIANKDSMHRQTE 360
Cdd:pfam07888  158 RAKKAGAQRKEeeaerkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   361 DKNRQLQERLELAEQKLqQTLRkaETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKN----QELQRARQRE 436
Cdd:pfam07888  237 EELRSLQERLNASERKV-EGLG--EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaQERETLQQSA 313

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894   437 KMNEEHNKRLSDTVDKLlsesNERLQlhlKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRL 515
Cdd:pfam07888  314 EADKDRIEKLSAELQRL----EERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
258-491 5.85e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  258 IDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS 337
Cdd:COG4913   666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  338 VH--DLNDKLENEIANK--DSMHRQTEDKNRQLQERLELAEQKLQQTLRKA-ETLPEVEAELAQRVAALSKAEERHGNIE 412
Cdd:COG4913   746 ELraLLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEYLALLDRLE 825

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894  413 erlrqmeaqleekNQELQRARQREKmneehnkrlsdtvdKLLSESNERLQLHLKERMAaledknsllREVENAKKQLEE 491
Cdd:COG4913   826 -------------EDGLPEYEERFK--------------ELLNENSIEFVADLLSKLR---------RAIREIKERIDP 868
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
253-456 6.18e-06

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 50.46  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  253 ELQEVIDRQAREQSQMKERLASLSSHAAELE---------EDLDTARKDLIKSEEMNTKLQrEVREAMAQKED-MEERIT 322
Cdd:COG0497   169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLREALQ-EALEALSGGEGgALDLLG 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  323 tlekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ----------ERLELAEQKLQ---QTLRK----AE 385
Cdd:COG0497   248 -------QALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvtVE 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  386 TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmneEHNKRLSDTVDKLLSE 456
Cdd:COG0497   321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
399-516 8.27e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 48.28  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  399 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--ALE 473
Cdd:COG1842    16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568952894  474 DKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:COG1842    92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
341-524 8.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  341 LNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME- 419
Cdd:COG4717    47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEk 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  420 ---------------AQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:COG4717   124 llqllplyqelealeAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568952894  485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGR 524
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 365-514 8.93e-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: 48.38  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  365 QLQERLELAE--QKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEh 442
Cdd:COG1579     5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894  443 nkrlsdtvdKLLSESNERLQLHLKERMAALEDKNSLLREVE-NAKKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG1579    81 ---------QLGNVRNNKEYEALQKEIESLKRRISDLEDEIlELMERIEELEEELAELEAELAELEAELEEKK 144
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-438 9.51e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 49.68  E-value: 9.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220    5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220   85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEV--IDRQ 261
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQ 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   262 AREQSQMKERLASLSSHAAE---LEEDLDTARKDLIKSEEMNTklqrevrEAMAQKEDMEERITTLEKRYLAAQREATSV 338
Cdd:pfam19220  223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   339 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 418
Cdd:pfam19220  296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 568952894   419 E-------AQLEEKNQELQRARQREKM 438
Cdd:pfam19220  359 TkrfeverAALEQANRRLKEELQRERA 385
PRK01156 PRK01156
chromosome segregation protein; Provisional
 175-485 9.79e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.90  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgLLDGNHEQESAPSTNGKRSSDGSLShEDLAKVLEL 254
Cdd:PRK01156  464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLE-DIKIKINEL 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  255 QEVIDRQareqSQMKERLASLSShaaeleEDLDTARKDLIKSeeMNTKLQREVREAMAQKEDMEERITTLEKRylaAQRE 334
Cdd:PRK01156  542 KDKHDKY----EEIKNRYKSLKL------EDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESR---LQEI 606

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  335 ATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErLELAEQKLQQTLrkaETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK01156  607 EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDN 682

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  415 LRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVENA 485
Cdd:PRK01156  683 LKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 251-516 1.02e-05

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: 50.17  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   251 VLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEErittlEKRYLa 330
Cdd:pfam01576  140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK-----AKRKL- 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   331 aQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET-LPEVEAELAQRVAALSKAEE 406
Cdd:pfam01576  214 -EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   407 RHGNIEERLRQMEAQLEEK------NQELQRARQRE-----KMNEEHNKRLsdtvDKLLSESNERLQLHLKERMAALEDK 475
Cdd:pfam01576  293 QRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkKALEEETRSH----EAQLQEMRQKHTQALEELTEQLEQA 368

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568952894   476 NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam01576  369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
254-514 1.05e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  254 LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQR 333
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  334 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 413
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  414 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQ 493
Cdd:COG4372   189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268

                         250       260
                  ....*....|....*....|.
gi 568952894  494 HDKDQLVVTIEALKAELEQMR 514
Cdd:COG4372   269 VEKDTEEEELEIAALELEALE 289
mukB PRK04863
chromosome partition protein MukB;
221-508 1.25e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.96  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  221 LDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDR--QAREQ----SQMKERLASLSSHAAELEEDLDTARKDli 294
Cdd:PRK04863  856 HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRveEIREQldeaEEAKRFVQQHGNALAQLEPIVSVLQSD-- 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  295 ksEEMNTKLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAE 374
Cdd:PRK04863  934 --PEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAAEMLA-----------KNSDLNEKLRQRLEQAE 998

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  375 QklqQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQEL---------QRARQREkmnEEHNKR 445
Cdd:PRK04863  999 Q---ERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQELKQELQDLgvpadsgaeERARARR---DELHAR 1068

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952894  446 LSDTvdkllsesnerlqlhlKERMAALEDKNSLL-REVENAKKQLEETQHDKDQLVVTIEALKA 508
Cdd:PRK04863 1069 LSAN----------------RSRRNQLEKQLTFCeAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 249-484 1.42e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 49.66  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   249 AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY 328
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   329 LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERH 408
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894   409 GNIEERLRQMEAQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVEN 484
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-485 1.53e-05

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: 49.58  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   127 HLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMIL 206
Cdd:pfam02463  676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   207 KEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:pfam02463  756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   287 DTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL 366
Cdd:pfam02463  836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   367 QERLELAEQKLQQTLRKAETLPEVEaeLAQRVAALSKAEERHGNIEERLRQMEAQLEEK-----NQELQRARQREKMNEE 441
Cdd:pfam02463  916 ENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNKD 993

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 568952894   442 H--NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam02463  994 EleKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-434 2.07e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717   228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  204 MILKEQNNQKKTltdglldgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLAsLSSHAAELE 283
Cdd:COG4717   305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIA 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  284 EDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDKN 363
Cdd:COG4717   374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEEL 448

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  364 RQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 434
Cdd:COG4717   449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 253-436 2.50e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqKEDMEERITTLEKRYLAAQ 332
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  333 R------------EATSVHDLNDKLEN--------------------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT 380
Cdd:COG3883    97 RsggsvsyldvllGSESFSDFLDRLSAlskiadadadlleelkadkaELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  381 LRKAE----TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3883   177 QAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 253-383 3.53e-05

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.05  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREA-MAQKEDMEERITTLEKRYLAA 331
Cdd:pfam15619   57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894   332 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 383
Cdd:pfam15619  137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 379-512 4.11e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  379 QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE----EHNKRLSDTVDKLL 454
Cdd:COG1579     4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieEVEARIKKYEEQLG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  455 SESNER----LQL---HLKERMAALEDK-NSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG1579    84 NVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1078-1148 4.36e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.64  E-value: 4.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  1078 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1148
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
259-434 4.58e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  259 DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIK----------SEEMNTKLQR------EVREAMAQKEDMEERIT 322
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  323 TLEKR------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE 393
Cdd:COG3206   244 ALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELE 323

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568952894  394 -LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 434
Cdd:COG3206   324 aLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
RNase_Y_N pfam12072
RNase Y N-terminal region;
364-511 5.42e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.65  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   364 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   428 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEnakkqlEETQHDKDQLVVTIE 504
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175


                   ....*..
gi 568952894   505 AlKAELE 511
Cdd:pfam12072  176 E-EAKEE 181
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 253-507 7.46e-05

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: 46.94  E-value: 7.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKS-------EEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikdlTNQDSVKELIIKNLDNTRESLETQLKVLS 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   326 KRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAE 405
Cdd:TIGR04523  475 RSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLE 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   406 ERHGNIEERLR--QMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED------- 474
Cdd:TIGR04523  545 DELNKDDFELKkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakk 624

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 568952894   475 ---------------KNSLLREVENAKKQLEETQHDKDQLVVTIEALK 507
Cdd:TIGR04523  625 eneklssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 281-521 9.66e-05

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: 46.89  E-value: 9.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   281 ELEEDLDTARKDLIKSEEMNTKlqREVREAMAQKEDMEERI----TTLEKRYLAAQREATSVHDLNDKLENEIANKDSMH 356
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   357 RQTEDKNRQLQERLELAEQKLQQTLRKAEtlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:pfam02463  235 NEERIDLLQELLRDEQEEIESSKQEIEKE-----EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   437 KMNEEhNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam02463  310 VDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388


                   ....*
gi 568952894   517 GPSLH 521
Cdd:pfam02463  389 AAKLK 393
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
363-502 1.02e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.81  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  363 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-------- 434
Cdd:COG1566    78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952894  435 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVT 502
Cdd:COG1566   147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 164-658 1.20e-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: 46.64  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   164 LKSLFEHHKALDEKVrERLRVALERC----SLLEEELGATHKELMILKEQnnqkktltdglldgnhEQESAPSTNGKRSS 239
Cdd:pfam05483  284 LKELIEKKDHLTKEL-EDIKMSLQRSmstqKALEEDLQIATKTICQLTEE----------------KEAQMEELNKAKAA 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   240 DGSLSHEDLAKVLELQEVI----DRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKL--QREVREAMAQ 313
Cdd:pfam05483  347 HSFVVTEFEATTCSLEELLrteqQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaeDEKLLDEKKQ 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   314 KEDMEERITTLEKR--YLAAQREaTSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-ERLELAEQKLQQTLRKAETlPEV 390
Cdd:pfam05483  427 FEKIAEELKGKEQEliFLLQARE-KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLEN-KEL 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   391 EAELAQRVAALSKAEERHGNIEERLRQMEAQLEE-KNQELQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERM 469
Cdd:pfam05483  505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENlEEKEMNLRDELESVREEF-IQKGDEVKCKLDKSEENARSIEYEVL 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   470 AALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALK----AELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGH---- 541
Cdd:pfam05483  584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYqkei 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   542 -VDAYSTSAVLRRPQKGRLAAlrDEPSKVQtlNEQDWERAQQASVLANVAQAFESDVD-VSDGEDDRDTLLSSVDLLSPS 619
Cdd:pfam05483  664 eDKKISEEKLLEEVEKAKAIA--DEAVKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDkIIEERDSELGLYKNKEQEQSS 739

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 568952894   620 GQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEE 658
Cdd:pfam05483  740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 320-516 1.32e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 44.98  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   320 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL------------ 387
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   388 -----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLLSESnerLQ 462
Cdd:pfam12795   76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894   463 LHLKERMAALEDKNSLLR-EVENA-------KKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam12795  152 WALQAELAALKAQIDMLEqELLSNnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 249-513 1.37e-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: 46.32  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   249 AKVLELQEVIDRQAR-EQSQMKERLASLSSHAAELEEDLDTARK---DLIKS----EEMNTKLQREVREAMAQKEDMEER 320
Cdd:pfam01576  327 QEVTELKKALEEETRsHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   321 -------ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN-----------RQLQERLELAEQKLQQTLR 382
Cdd:pfam01576  407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvssleSQLQDTQELLQEETRQKLN 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   383 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL--------- 453
Cdd:pfam01576  487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqqleekaa 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   454 ----LSESNERLQLHLKERMAALEDKNSLLREVENAKKQ---------------------------------------LE 490
Cdd:pfam01576  567 aydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfdqmlaeekaisaryaeerdraeaeareketralslaraLE 646

                          330       340
                   ....*....|....*....|...
gi 568952894   491 ETQHDKDQLVVTIEALKAELEQM 513
Cdd:pfam01576  647 EALEAKEELERTNKQLRAEMEDL 669
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 246-494 1.60e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.12  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQevidRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLE 325
Cdd:TIGR00618  273 RAQEAVLEET----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   326 KRYLAAQReatsvhdLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS- 402
Cdd:TIGR00618  349 TLHSQEIH-------IRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRd 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   403 -KAEERHGNIEERLRQMEAQLEEknQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 481
Cdd:TIGR00618  422 lQGQLAHAKKQQELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499

                          250
                   ....*....|...
gi 568952894   482 VENAKKQLEETQH 494
Cdd:TIGR00618  500 QEEPCPLCGSCIH 512
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 248-514 1.91e-04

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: 46.10  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  248 LAKVLELQEVIDR--QAREQ-SQMKERLASLSSH---AAELEEDLDTARKDLIKSEEmntkLQREVREAMAQKEDMEERI 321
Cdd:COG3096   882 QANLLADETLADRleELREElDAAQEAQAFIQQHgkaLAQLEPLVAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQQI 957

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  322 TTLEkrYLAAQREATSVHDLNDKLEneiankdsmhrQTEDKNRQLQERLELAEQklqqtlrkaetlpeveaelaqrvaAL 401
Cdd:COG3096   958 FALS--EVVQRRPHFSYEDAVGLLG-----------ENSDLNEKLRARLEQAEE------------------------AR 1000

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  402 SKAEERhgnieerLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNS 477
Cdd:COG3096  1001 REAREQ-------LRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRS 1073

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568952894  478 LLREVEnakKQLEETQHDKDQLVVTIEALKAELEQMR 514
Cdd:COG3096  1074 RRSQLE---KQLTRCEAEMDSLQKRLRKAERDYKQER 1107
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1000-1055 1.92e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.72  E-value: 1.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894  1000 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1055
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 887-945 1.97e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 40.78  E-value: 1.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894  887 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 945
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
250-421 2.14e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  250 KVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQR--EVREAMAQKEDMEERITTLEKR 327
Cdd:COG3206   206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  328 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEE 406
Cdd:COG3206   286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365

                         170
                  ....*....|....*
gi 568952894  407 RHGNIEERLRQMEAQ 421
Cdd:COG3206   366 LYESLLQRLEEARLA 380
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 342-446 2.40e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  342 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 416
Cdd:PRK00409  515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568952894  417 QMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 446
Cdd:PRK00409  595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 36-497 2.80e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    36 FEQLMVSMLEERDRLLDTLRETQ--ETLALTQGKLHEVGH-ERDSLQRQ---LNTALPQEFAALTKELNVCREQLLEREE 109
Cdd:TIGR00618  154 FAQFLKAKSKEKKELLMNLFPLDqyTQLALMEFAKKKSLHgKAELLTLRsqlLTLCTPCMPDTYHERKQVLEKELKHLRE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   110 EIAELKAERNNTRLLLEHLECLVSRHE--RSLRMTVVKRQAQSPAGVSSEVEVLKALKS--LFEHHKALDEKVRERLRVA 185
Cdd:TIGR00618  234 ALQQTQQSHAYLTQKREAQEEQLKKQQllKQLRARIEELRAQEAVLEETQERINRARKAapLAAHIKAVTQIEQQAQRIH 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   186 LERCSLLEEELGATHKELMILKEQNN--QKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDrQAR 263
Cdd:TIGR00618  314 TELQSKMRSRAKLLMKRAAHVKQQSSieEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLT 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   264 EQSQMKERLASLSSHAAELEEDLDTARKDL---IKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATsvhd 340
Cdd:TIGR00618  393 QKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL---- 468

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   341 lnDKLENEIANKDSMHRQTEDKNRQLQERLELaEQKLQQTLRKAETLPEVEAELAQRVAALS----KAEERHGNIEERLR 416
Cdd:TIGR00618  469 --KEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqRGEQTYAQLETSEE 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   417 QMEAQL-EEKNQ------ELQRARQREKMNEEHNKRLSDTVDKLLSEsnerLQLHLKERMAALEDKNSLLREVENAKKQL 489
Cdd:TIGR00618  546 DVYHQLtSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNI----TVRLQDLTEKLSEAEDMLACEQHALLRKL 621


                   ....*...
gi 568952894   490 EETQHDKD 497
Cdd:TIGR00618  622 QPEQDLQD 629
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 163-441 2.95e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.20  E-value: 2.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   163 ALKSLFEhhkALDEKVR--ERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTD---GLLD-GNHEQESAPSTN 234
Cdd:pfam10174  437 ALTTLEE---ALSEKERiiERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEkesSLIDlKEHASSLASSGL 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   235 GKRSSDGSL-----SHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHaaeLEEDLDTARKDLIKSEEMNTKLQREVRE 309
Cdd:pfam10174  514 KKDSKLKSLeiaveQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL---LEQEVARYKEESGKAQAEVERLLGILRE 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   310 AMAQKEDMEERITTLEKRYLAAQREATSvhdlndklenEIANKDSMhrQTEDKNRQLQErlelaeqkLQQTLRKAETLPE 389
Cdd:pfam10174  591 VENEKNDKDKKIAELESLTLRQMKEQNK----------KVANIKHG--QQEMKKKGAQL--------LEEARRREDNLAD 650

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568952894   390 VEAE--LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-REKMNEE 441
Cdd:pfam10174  651 NSQQlqLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAeRRKQLEE 705
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 267-430 2.96e-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: 43.02  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   267 QMKERLASLSSHAAELEEDLDTARKDLIK---------SEEMNTKLQrEVREAMAQK-EDMEERIT-TLEKrylAAQREA 335
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQELVDrleketealRERLQKDLE-EVRAKLEPYlEELQAKLGqNVEE---LRQRLE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   336 TSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAQRVAALSK-----AEERHGN 410
Cdd:pfam01442   77 PYTEELRKRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELKEslapyAEEVQAQ 151

                          170       180
                   ....*....|....*....|
gi 568952894   411 IEERLRQMEAQLEEKNQELQ 430
Cdd:pfam01442  152 LSQRLQELREKLEPQAEDLR 171
PTZ00121 PTZ00121
MAEBL; Provisional
 295-512 3.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  295 KSEEMNTKLQREVREAMAQKED---MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLE 371
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARK 1183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  372 LAEQKLQQTLRKAETLPEVEA----------------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRAR-- 433
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARma 1263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  434 ---QREKMNEEHNKRLSDTVDKL--------LSESNERLQL-HLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVV 501
Cdd:PTZ00121 1264 hfaRRQAAIKAEEARKADELKKAeekkkadeAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343

                         250
                  ....*....|.
gi 568952894  502 TIEALKAELEQ 512
Cdd:PTZ00121 1344 AAEAAKAEAEA 1354
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 45-427 3.31e-04

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: 45.33  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   45 EERDRLLD-------TLRETQETLALTQGKLHEVGHERDSLQRQlNTALPQEFAALTKELNVCREQLLER------EEEI 111
Cdd:COG3096   278 NERRELSEralelrrELFGARRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQQekieryQEDL 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  112 AELkAERnntrlLLEHLECLVSRHERSLRmtvvkRQAQSPAgvsSEVEVlKALKS-LFEHHKALDE---------KVRER 181
Cdd:COG3096   357 EEL-TER-----LEEQEEVVEEAAEQLAE-----AEARLEA---AEEEV-DSLKSqLADYQQALDVqqtraiqyqQAVQA 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  182 LRVALERCSLLEEELGATHKELMILKEQNNQkktLTDGLLDGNHeqesapstngkRSSDGSLSHEDLAKVLELQEVID-- 259
Cdd:COG3096   422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQ---ATEEVLELEQ-----------KLSVADAARRQFEKAYELVCKIAge 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 --------------RQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAmaqkEDMEERITTLE 325
Cdd:COG3096   488 versqawqtarellRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELE 563

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  326 krylaAQREatsvhDLNDKLENEIANKDSMHRQTEDKNRQ-------------LQERLE-LAEQkLQQTLrkaETLPEVE 391
Cdd:COG3096   564 -----AQLE-----ELEEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALErLREQ-SGEAL---ADSQEVT 629

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 568952894  392 AELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 427
Cdd:COG3096   630 AAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 176-517 3.44e-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: 44.73  E-value: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLldGNHEQESAPSTNgkrssdgslSHEDLAKVLELQ 255
Cdd:pfam05557  135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKN---------SKSELARIPELE 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   256 EVIDRQAREQSQ---MKERLASLSSHAAELEEDLDT---ARKDLIKSEEMNTKLQREVRE----------AMAQKEDMEE 319
Cdd:pfam05557  204 KELERLREHNKHlneNIENKLLLKEEVEDLKRKLEReekYREEAATLELEKEKLEQELQSwvklaqdtglNLRSPEDLSR 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   320 RITTLEKRYLAAQREATSVhdlndkleneiankDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVA 399
Cdd:pfam05557  284 RIEQLQQREIVLKEENSSL--------------TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   400 ALSKaeERHGnIEERLRQMEAQLEEKN---QELQRARQREKMNEE---HNKRLSDTVDKLLSE--------SNERLQLHL 465
Cdd:pfam05557  350 LLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMTQKmqaHNEEMEAQLSVAEEElggykqqaQTLERELQA 426

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568952894   466 KERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:pfam05557  427 LRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 193-514 4.05e-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: 44.78  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   193 EEELGATHKELMILKEQNNQ-KKTLTDglLDGNHEQESAPST--NGKRSSDGSLSHED-------LAKVLELQEVI---- 258
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKaESELKE--LEKKHQQLCEEKNalQEQLQAETELCAEAeemrarlAARKQELEEILhele 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   259 ----DRQAREQSQMKERlASLSSHAAELEEDLD---TARK------------------DLIKSEEMNTKLQREvreamaq 313
Cdd:pfam01576   82 srleEEEERSQQLQNEK-KKMQQHIQDLEEQLDeeeAARQklqlekvtteakikkleeDILLLEDQNSKLSKE------- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   314 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQtEDKNRQLQERL---------ELAEQKLQQTLRKA 384
Cdd:pfam01576  154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestDLQEQIAELQAQIA 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   385 ETLPEVEAELAQRVAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEsnerL 461
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE----L 308

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894   462 QLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVV--------TIEALKAELEQMR 514
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQemrqkhtqALEELTEQLEQAK 369
46 PHA02562
endonuclease subunit; Provisional
 281-500 4.10e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  281 ELEEDLDT--ARKDLIKSE-EMNTKLQREVREAMAQkedmeeRITTLEKRYLAAQREATSVHDLNDKLENEIANKD-SMH 356
Cdd:PHA02562  178 ELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmDIE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  357 RQTEDKNRQLQERLELAEQ-----KLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQ-MEAQLEEKNQELQ 430
Cdd:PHA02562  252 DPSAALNKLNTAAAKIKSKieqfqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKlDTAIDELEEIMDE 331

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  431 RARQREKMNEEHNK-RLSDTVDKLLSESNERLQLHLKERMAALEDKNSllrEVENAKKQLEETQHDKDQLV 500
Cdd:PHA02562  332 FNEQSKKLLELKNKiSTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE---ELAKLQDELDKIVKTKSELV 399
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 264-428 4.33e-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: 42.97  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   264 EQSQMKERLASLSSHAAELEEDLDTARKD---LIKSEEMNTKLQREVREAMAQKEDMEERIttlekrylaaqreatsvhd 340
Cdd:pfam13851   55 ENKRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLEQRF------------------- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   341 lnDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMe 419
Cdd:pfam13851  116 --EKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV- 189


                   ....*....
gi 568952894   420 aqLEEKNQE 428
Cdd:pfam13851  190 --LESKNQL 196
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 260-519 4.71e-04

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: 44.56  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  260 RQAREQsqmkeRLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ--KEDMEERITTLEKRylaaQREats 337
Cdd:COG3096   780 RAAREK-----RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVafAPDPEAELAALRQR----RSE--- 847

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  338 vhdlndkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQT-LRKAETLPEVEAELAQRVAALSKAE---ERHGNIEE 413
Cdd:COG3096   848 -------LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnLLADETLADRLEELREELDAAQEAQafiQQHGKALA 920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  414 RLR--------------QMEAQLEEKNQELQRARQR-EKMNEEHNKRL----SDTVDkLLSESNErLQLHLKERMAALED 474
Cdd:COG3096   921 QLEplvavlqsdpeqfeQLQADYLQAKEQQRRLKQQiFALSEVVQRRPhfsyEDAVG-LLGENSD-LNEKLRARLEQAEE 998

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  475 KNSLLRE-VENAKKQLEE---------TQHD-KDQlvvTIEALKAELEQMRLRGPS 519
Cdd:COG3096   999 ARREAREqLRQAQAQYSQynqvlaslkSSRDaKQQ---TLQELEQELEELGVQADA 1051
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
344-510 5.74e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 42.89  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  344 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEER 414
Cdd:COG1842    41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  415 LRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAK---KQLEE 491
Cdd:COG1842   121 LRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAE 199

                         170       180
                  ....*....|....*....|..
gi 568952894  492 TQHDK---DQLvvtiEALKAEL 510
Cdd:COG1842   200 LEADSeveDEL----AALKAKM 217
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 154-512 6.02e-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: 44.40  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   154 VSSEVEVLKALKSLFEHHKALDEKVRErLRVALERcslLEEELGATH------------------KELMILKEQNNQKKT 215
Cdd:pfam01576  670 VSSKDDVGKNVHELERSKRALEQQVEE-MKTQLEE---LEDELQATEdaklrlevnmqalkaqfeRDLQARDEQGEEKRR 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   216 LtdgLLDGNHEQESAPSTNGKRSSDGSLSHEDLA---KVLELQEVIDRQAREQS--QMKERLASLSSHAAELEEDLDTAR 290
Cdd:pfam01576  746 Q---LVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRD 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   291 KDLIKSEEMNTKLQrevreamaqkeDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERL 370
Cdd:pfam01576  823 EILAQSKESEKKLK-----------NLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   371 ELAEQKLQQTLRKAETLPEVEAELAQRVAALS---KAEERHGNIEERLRQmeaQLEEKNQELQ-RARQREKMNEEHNKRL 446
Cdd:pfam01576  892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTSQKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSS 968

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   447 SDTVDKLLSESNERLQLHLKERMAA---LEDKNSLLRE----VENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:pfam01576  969 IAALEAKIAQLEEQLEQESRERQAAnklVRRTEKKLKEvllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 343-508 6.51e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.36  E-value: 6.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   343 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAE----------------TLPEVEAELAQRVAALSKAEE 406
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   407 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENA- 485
Cdd:pfam04012  119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELASAv 190

                          170       180
                   ....*....|....*....|....*
gi 568952894   486 --KKQLEETQHDKDQLVVTIEALKA 508
Cdd:pfam04012  191 dlDAKLEQAGIQMEVSEDVLARLKA 215
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-352 7.76e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  162 KALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRS 238
Cdd:COG4942    48 KEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  239 SDGSLsheDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDM 317
Cdd:COG4942   128 PEDFL---DAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568952894  318 EERITTLEKRYLAAQREATSVHDLNDKLENEIANK 352
Cdd:COG4942   205 EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 246-459 9.03e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  246 EDLAKVLElQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARK-------DLIKSEEMNT-KLQREVREAMAQKEDM 317
Cdd:PRK05771   34 EDLKEELS-NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKELEEEISEL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  318 EERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEQKLQQTLRK-------------A 384
Cdd:PRK05771  113 ENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlK 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894  385 ETLPEVEAELAQrvAALSKAE-ERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDKLLSESNE 459
Cdd:PRK05771  188 ELSDEVEEELKK--LGFERLElEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELER 262
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 139-662 9.64e-04

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: 43.50  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   139 LRMTVVKRQAQspagVSSEVEVLKALKSLFEHHKALDEKVRERLRVALErcslLEEELGATHKELMILKEQNNQKKTLTD 218
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKDNSELELKME 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   219 GLLDGNHEQESAPSTNgkRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERL---ASLSSHAAELEEDLDTARKDLIK 295
Cdd:TIGR00606  294 KVFQGTDEQLNDLYHN--HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlveQGRLQLQADRHQEHIRARDSLIQ 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   296 SEEMNTKL---------QREVREAMA-QKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 365
Cdd:TIGR00606  372 SLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   366 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE--HN 443
Cdd:TIGR00606  452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHH 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   444 KRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENaKKQLEETQHDK-DQLVVTIEALK------AELEQMRlr 516
Cdd:TIGR00606  531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKsKEINQTRDRLAklnkelASLEQNK-- 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   517 gpslHHGRPHLGSVPDFRFSVADGHVDAYSTsavlrrpqkgrlaalRDEPSKVQTLNEQDWERAQQASVLANVAQAFESD 596
Cdd:TIGR00606  608 ----NHINNELESKEEQLSSYEDKLFDVCGS---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894   597 VDVSDGEDDRdtllssvdlLSPSGQADAQTLAmMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 662
Cdd:TIGR00606  669 ITQLTDENQS---------CCPVCQRVFQTEA-ELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 113-524 9.68e-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: 43.63  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   113 ELKAERNNTRLLLEH-LECLVSRHERSLRmTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKvrERLRVALERCSL 191
Cdd:pfam01576  320 ELRSKREQEVTELKKaLEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES--ENAELQAELRTL 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   192 LEEELGATHK---------ELMI-LKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKV-LELQeviDR 260
Cdd:pfam01576  397 QQAKQDSEHKrkklegqlqELQArLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQ---DT 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   261 QAREQSQMKERLaSLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQ----KEDMEERITTLEKRYLAAQREAT 336
Cdd:pfam01576  474 QELLQEETRQKL-NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlsdmKKKLEEDAGTLEALEEGKKRLQR 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   337 SVHDLNDKLENEIANKDSMHRQTE-------------DKNRQLQERLELAEQKLQQTL--------RKAETLPEVEAELA 395
Cdd:pfam01576  553 ELEALTQQLEEKAAAYDKLEKTKNrlqqelddllvdlDHQRQLVSNLEKKQKKFDQMLaeekaisaRYAEERDRAEAEAR 632

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   396 QRVA-------ALSKAEERHGNIEERLRQMEAQLEE---------KN-QELQRA-RQREKMNEEHNKRLSDTVDKLLSES 457
Cdd:pfam01576  633 EKETralslarALEEALEAKEELERTNKQLRAEMEDlvsskddvgKNvHELERSkRALEQQVEEMKTQLEELEDELQATE 712

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   458 NERLQLHLKerMAAL----------------EDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:pfam01576  713 DAKLRLEVN--MQALkaqferdlqardeqgeEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAN 790


                   ...
gi 568952894   522 HGR 524
Cdd:pfam01576  791 KGR 793
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-521 1.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  253 ELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ 332
Cdd:COG4372    70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  333 REATSVHDLNDKLENEIAN--KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS--KAEERH 408
Cdd:COG4372   150 EELKELEEQLESLQEELAAleQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  409 GNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQ 488
Cdd:COG4372   230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309

                         250       260       270
                  ....*....|....*....|....*....|...
gi 568952894  489 LEETQHDKDQLVVTIEALKAELEQMRLRGPSLH 521
Cdd:COG4372   310 IGALEDALLAALLELAKKLELALAILLAELADL 342
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 357-513 1.12e-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: 43.40  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  357 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 436
Cdd:COG3096   525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894  437 KMNEEHNKRLsdtvdkllsesnERLQLHLKErmaALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQM 513
Cdd:COG3096   602 PAWLAAQDAL------------ERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-473 1.12e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921  321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921  401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKEQNNQK-KTLTDGLLDGNHEQESAPSTNGKRssdgs 242
Cdd:pfam15921  480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALK----- 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   243 LSHEDLAKVLE-LQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEeri 321
Cdd:pfam15921  555 LQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--- 631

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   322 ttLEKRYL--AAQREATSVHDLN---DKLENEIAN-KDSMHRQTEDKN------RQLQERLELAEQKLQQTLRKAET--- 386
Cdd:pfam15921  632 --LEKVKLvnAGSERLRAVKDIKqerDQLLNEVKTsRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSele 709

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   387 ---------------------------------------------------------LPEVEAELAQRVAALSKAEERHG 409
Cdd:pfam15921  710 qtrntlksmegsdghamkvamgmqkqitakrgqidalqskiqfleeamtnankekhfLKEEKNKLSQELSTVATEKNKMA 789

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952894   410 NIEERLRQMEAQLEEKNQELQRARQREKMneehnkRLSDTVDKLLSESNERLQLHLKERMAALE 473
Cdd:pfam15921  790 GELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 323-444 1.32e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.96  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  323 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 389
Cdd:cd07680    61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568952894  390 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 444
Cdd:cd07680   141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 174-512 1.32e-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: 43.02  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  174 LDEKVRERL---RVALERCSLLEEELgaTHKELMILKEqnNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDL-- 248
Cdd:COG5185   143 LDEIADIEAsygEVETGIIKDIFGKL--TQELNQNLKK--LEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGse 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  249 ------AKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTAR-KDLIKSEEMNTKLQREVREAMAQKEDMEERI 321
Cdd:COG5185   219 stllekAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKI 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  322 TTLEKrylaaqreatsvhdlndkleneianKDSMHRQTEDKNRQLQERLElaEQKLQQTLRKAET-LPEVEAELAQRVAA 400
Cdd:COG5185   299 AEYTK-------------------------SIDIKKATESLEEQLAAAEA--EQELEESKRETETgIQNLTAEIEQGQES 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  401 LSKAEERHGN-------------IEERLRQMEAQLEEKNQELQRARQ-REKMNEEHNKRLSDTVdKLLSESNERLQlhlk 466
Cdd:COG5185   352 LTENLEAIKEeienivgevelskSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDTL-KAADRQIEELQ---- 426

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 568952894  467 ermAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQ 512
Cdd:COG5185   427 ---RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
mukB PRK04863
chromosome partition protein MukB;
112-487 1.56e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  112 AELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspagvssevEVLKALKSLFEHHKaldeKVRERL 182
Cdd:PRK04863  803 ATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELERALADHESQEQ----QQRSQL 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  183 RVALERCSLLEEELGathkELMILKEQnnqkkTLTDGLLDgnheqesapstngkrssdgslSHEDLAKVLELQEVIDRQA 262
Cdd:PRK04863  868 EQAKEGLSALNRLLP----RLNLLADE-----TLADRVEE---------------------IREQLDEAEEAKRFVQQHG 917

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  263 REQSQMKERLASLSSHAAELEEdldtarkdlikseemntkLQREVREAMAQKEDMEERITTLEkrYLAAQREATSVHDLN 342
Cdd:PRK04863  918 NALAQLEPIVSVLQSDPEQFEQ------------------LKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDAA 977

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  343 DKLEneiankdsmhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQL 422
Cdd:PRK04863  978 EMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQEL 1039

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  423 EEKNQEL---------QRARQREkmnEEHNKRLSDT------VDKLLSESNERLQlHLKERMAALEDKNSLLRE-VENAK 486
Cdd:PRK04863 1040 KQELQDLgvpadsgaeERARARR---DELHARLSANrsrrnqLEKQLTFCEAEMD-NLTKKLRKLERDYHEMREqVVNAK 1115


                  .
gi 568952894  487 K 487
Cdd:PRK04863 1116 A 1116
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 886-948 1.65e-03

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.02  E-value: 1.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568952894   886 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 948
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
mukB PRK04863
chromosome partition protein MukB;
325-517 1.67e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  325 EKRYLAAQREAtsvhdlndkLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 404
Cdd:PRK04863  507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  405 EERHGNIEERLRQMEAQLEEKNQELQRARQrekmnEEHNkrlsdtvdklLSESNERLQLHLKErmaALEDKNSLLREVEN 484
Cdd:PRK04863  574 VSEARERRMALRQQLEQLQARIQRLAARAP-----AWLA----------AQDALARLREQSGE---EFEDSQDVTEYMQQ 635

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568952894  485 AKKQLEETQHDKDQLVVTIEALKAELEQMRLRG 517
Cdd:PRK04863  636 LLERERELTVERDELAARKQALDEEIERLSQPG 668
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 1000-1047 1.70e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 38.05  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568952894 1000 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1047
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
PRK12704 PRK12704
phosphodiesterase; Provisional
 364-514 1.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  364 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMNEEHn 443
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  444 krlsdtvdkllsesnerlqlhLKERMAALEDKNSLLREVENAKKQLEETqhdkdqlvvtIEALKAELEQMR 514
Cdd:PRK12704   98 ---------------------LDRKLELLEKREEELEKKEKELEQKQQE----------LEKKEEELEELI 137
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1076-1142 1.76e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 38.02  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568952894 1076 RDVLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1142
Cdd:cd09512     2 RPVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
46 PHA02562
endonuclease subunit; Provisional
 207-430 1.78e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  207 KEQNNQKKTLtDGLLDGNHEQESAPSTNGKRSSdgSLSHEDLAkvlELQEVIDRQAREQSQMKERLASLSSHAAELEEDL 286
Cdd:PHA02562  177 RELNQQIQTL-DMKIDHIQQQIKTYNKNIEEQR--KKNGENIA---RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  287 DTARKDLIKSEEMNTKLQREV----REA------------MAQKEDMEERITTLEKRYLAAQreaTSVHDLNDKLENEIA 350
Cdd:PHA02562  251 EDPSAALNKLNTAAAKIKSKIeqfqKVIkmyekggvcptcTQQISEGPDRITKIKDKLKELQ---HSLEKLDTAIDELEE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  351 NKDSMHRQTEdKNRQLQERLELAEQKLQQTLRKAEtlpEVEAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQ 430
Cdd:PHA02562  328 IMDEFNEQSK-KLLELKNKISTNKQSLITLVDKAK---KVKAA-------IEELQAEFVDNAEELAKLQDELDKIVKTKS 396
Caldesmon pfam02029
Caldesmon;
174-470 2.20e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   174 LDEKVRERLRVALERCSLLEEELGATHKELMILKEQNN-------QKKTLTDGLLDGNHEQESapSTNGKRSSDGSLSHE 246
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEKESVAERKENNEeeensswEKEEKRDSRLGRYKEEET--EIREKEYQENKWSTE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   247 DLAKVLELQEVIDRQAREQSQMKERlaslssHAAElEEDLDTARKDLIKSEEMNTKLQREVR---EAMAQKEDMEERITT 323
Cdd:pfam02029  149 VRQAEEEGEEEEDKSEEAEEVPTEN------FAKE-EVKDEKIKKEKKVKYESKVFLDQKRGhpeVKSQNGEEEVTKLKV 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   324 LEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpeVEAELAQRvaalsK 403
Cdd:pfam02029  222 TTKRRQGGLSQS-------QEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAE----LELEELKK-----K 285

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894   404 AEERHGNIEERLRQMEAqlEEKnqelqrarQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMA 470
Cdd:pfam02029  286 REERRKLLEEEEQRRKQ--EEA--------ERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
PLN02939 PLN02939
transferase, transferring glycosyl groups
 179-518 2.25e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.20  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  179 RERLRVAlerCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQE-------SAPSTNGKRSSDGSLSHEDLAKV 251
Cdd:PLN02939   28 RRRLAVS---CRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQlentslrTVMELPQKSTSSDDDHNRASMQR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  252 LELQEVIDRQAREQSQMKERLASLssHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY--- 328
Cdd:PLN02939  105 DEAIAAIDNEQQTNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLset 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  329 -----LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK--AETLPEVEAELAQRVAAL 401
Cdd:PLN02939  183 darikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKddIQFLKAELIEVAETEERV 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  402 SKAEERHGNIEERLRQMEAQLE------------------EKNQELQRARQREKMNEEH-------NKRLSDTVDKL--- 453
Cdd:PLN02939  260 FKLEKERSLLDASLRELESKFIvaqedvsklsplqydcwwEKVENLQDLLDRATNQVEKaalvldqNQDLRDKVDKLeas 339

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952894  454 LSESN------ERLQLhLKERMAALEDKnsLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGP 518
Cdd:PLN02939  340 LKEANvskfssYKVEL-LQQKLKLLEER--LQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 246-491 2.30e-03

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: 41.83  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQEVIDRQAREQSQMKERLAslsshAAELEEDLDTARKDLIKSEEMNtKLQREVREAMAQKEDMEERITTLE 325
Cdd:pfam13868  120 EKLEKQRQLREEIDEFNEEQAEWKELEK-----EEEREEDERILEYLKEKAEREE-EREAEREEIEEEKEREIARLRAQQ 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   326 KRYLAAQREATsvhDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETlpeveaelaqrvaalsKAE 405
Cdd:pfam13868  194 EKAQDEKAERD---ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR----------------LAE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   406 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllsesNERLQLHLKERMAALEDKNSLLREVENA 485
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI-------EEREEQRAAEREEELEEGERLREEEAER 327


                   ....*.
gi 568952894   486 KKQLEE 491
Cdd:pfam13868  328 RERIEE 333
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-276 2.90e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942    99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952894  202 ELM-ILKEQNNQKKTLTDGLLDgnhEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLS 276
Cdd:COG4942   175 ELEaLLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 284-512 3.42e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   284 EDLDTARKDLIKSEEMN----TKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQT 359
Cdd:TIGR04523   78 KILEQQIKDLNDKLKKNkdkiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   360 EDKNRQLQERLELAEQKL----QQTLRKAETLPEVEAELAQRVAALSKAEERhgniEERLRQMEAQLEE-KNQELQRARQ 434
Cdd:TIGR04523  158 NNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKK----IQKNKSLESQISElKKQNNQLKDN 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   435 REKMNEEHNKR---LSDTVDKLLSESNErlQLHLKERmaaLEDKNSllrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:TIGR04523  234 IEKKQQEINEKtteISNTQTQLNQLKDE--QNKIKKQ---LSEKQK---ELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305


                   .
gi 568952894   512 Q 512
Cdd:TIGR04523  306 Q 306
PRK12705 PRK12705
hypothetical protein; Provisional
 364-515 3.62e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  364 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMNEEHN 443
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  444 KRLSDTVDKLLSESNerlqlHLKERMAALEDKNSLLREV---------ENAKKQL-----EETQHDKDQLVVTIEAlKAE 509
Cdd:PRK12705   98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDNElyrvagltpEQARKLLlklldAELEEEKAQRVKKIEE-EAD 171


                  ....*.
gi 568952894  510 LEQMRL 515
Cdd:PRK12705  172 LEAERK 177
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 246-446 3.81e-03

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: 41.06  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   246 EDLAKVLELQEVIDRQAREQSQMKER--LASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITT 323
Cdd:pfam13868  130 EEIDEFNEEQAEWKELEKEEEREEDEriLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   324 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:pfam13868  210 LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568952894   404 A---------EERHgniEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRL 446
Cdd:pfam13868  290 EhrrelekqiEERE---EQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 271-514 4.50e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.99  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   271 RLASLSSHAAELEEDLD------------TARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRY------LAAQ 332
Cdd:pfam06160   61 SLPDIEELLFEAEELNDkyrfkkakkaldEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYrelrktLLAN 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   333 REA--TSVHDLNDKLEN--------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQT---LRKAET-LPEVEAELAQRV 398
Cdd:pfam06160  141 RFSygPAIDELEKQLAEieeefsqfEELTESGDYLEAREVLEKLEEETDALEELMEDIpplYEELKTeLPDQLEELKEGY 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   399 AALSKAEER--HGNIEERLRQMEAQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDKLLSESNERLQLHlkERMAA 471
Cdd:pfam06160  221 REMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVE--KNLPE 295

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568952894   472 LEDknsllrEVENAKKQLEETQHDKDQL----------VVTIEALKAELEQMR 514
Cdd:pfam06160  296 IED------YLEHAEEQNKELKEELERVqqsytlneneLERVRGLEKQLEELE 342
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 389-660 4.68e-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: 41.21  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   389 EVEAELAQRVAALSKAEERhgniEERLRQMeaqLEEKNQELQR-ARQREKMNEehnkrlsdtVDKLLSESNE-RLQLHLK 466
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEEN----IERLDLI---IDEKRQQLERlRREREKAER---------YQALLKEKREyEGYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   467 ERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRphlgsVPDFRFSVADGHVD--- 543
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE-----QLRVKEKIGELEAEias 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   544 AYSTSAVLRRPQK---GRLAALRDEPSKVQ-TLNEQDWERAQQASVLANVAQAFESDvdvsdgEDDRDTLLSSVDLLSPS 619
Cdd:TIGR02169  306 LERSIAEKERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEVDKE 379

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 568952894   620 GQA------DAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIE 660
Cdd:TIGR02169  380 FAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
PRK09039 PRK09039
peptidoglycan -binding protein;
255-433 5.12e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  255 QEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRyLAAQRe 334
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-LDSEK- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  335 ATSVHDLndkleneiankdsmhRQTEDKNRQLQErlelaeqklqqtLRkaetlpeveAELAQRVAALSKAEERHGNIEER 414
Cdd:PRK09039  130 QVSARAL---------------AQVELLNQQIAA------------LR---------RQLAALEAALDASEKRDRESQAK 173

                         170       180
                  ....*....|....*....|...
gi 568952894  415 L----RQMEAQLEEKNQELQRAR 433
Cdd:PRK09039  174 IadlgRRLNVALAQRVQELNRYR 196
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 320-516 5.79e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   320 RITTLEKRYLAAQREATSVHDL----NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPE------ 389
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAqeaaNRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkykels 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   390 -VEAELAQRVAALSKAEERHG----NIEERLRQMEAQLEEKNQELQRARQREKM------NEEHNKRLSDTVDKLLSESN 458
Cdd:pfam07888  108 aSSEELSEEKDALLAQRAAHEarirELEEDIKTLTQRVLERETELERMKERAKKagaqrkEEEAERKQLQAKLQQTEEEL 187

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568952894   459 ERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLR 516
Cdd:pfam07888  188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQER 245
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 249-513 6.07e-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: 40.88  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   249 AKVLELQEVIDRQAREQSQM----KERLASLSSHAAELEEDLDTARKdliKSEEMNTKLQ----REVREAMAQKEDMEEr 320
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   321 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 378
Cdd:pfam05557   78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   379 QTLRKAETLPEVEA---ELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARqrekmneEHNKRLSDTVDK--L 453
Cdd:pfam05557  157 NLEKQQSSLAEAEQrikELEFEIQSQEQDSEIVKNSKSEL----ARIPELEKELERLR-------EHNKHLNENIENklL 225

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952894   454 LSESNERLQLHL------KERMAALEDKNS-LLREVENAKKQLEETQHDkdqlVVTIEALKAELEQM 513
Cdd:pfam05557  226 LKEEVEDLKRKLereekyREEAATLELEKEkLEQELQSWVKLAQDTGLN----LRSPEDLSRRIEQL 288
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 260-491 6.68e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 40.59  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   260 RQAREQSQMKERLASLSShaaeLEEDLdtARKDLIKseemntKLQREVREAMAQKEDMEERITTLEKRYLAAQREATS-- 337
Cdd:pfam15066  292 QENCKTPDTEQSFESLQP----LEEDM--ALNEVLQ------KLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKqq 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   338 -----VHDLNDKLENEIANKDSMHRQTEDKNRQLQ---ERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHG 409
Cdd:pfam15066  360 vfvdiINKLKENVEELIEDKYNVILEKNDINKTLQnlqEILANTQKHLQESRKEKETL---QLELKKIKVNYVHLQERYI 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   410 N-IEERLR------QMEAQLEEKNQELQRARQrekMNEEHNKRLSDTVDKLLSESNERLQ--LHLKERMAALEDKNslLR 480
Cdd:pfam15066  437 TeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATTSALDLLKREKETREQefLSLQEEFQKHEKEN--LE 511

                          250
                   ....*....|.
gi 568952894   481 EVENAKKQLEE 491
Cdd:pfam15066  512 ERQKLKSRLEK 522
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
296-511 6.69e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  296 SEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ 375
Cdd:COG4372     1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  376 KLQQTlrkaetlpevEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTV---DK 452
Cdd:COG4372    81 ELEEL----------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaerEE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952894  453 LLSESNERLQlHLKERMAALEDKNSLLrEVENAKKQLEETQHDKDQLVVTIEALKAELE 511
Cdd:COG4372   151 ELKELEEQLE-SLQEELAALEQELQAL-SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
280-396 7.85e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.42  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  280 AELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQ---REATSVHDLNDklENEIANKDSMH 356
Cdd:COG1842    94 AELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaqeKVNEALSGIDS--DDATSALERME 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568952894  357 RQTEDKNRQLQERLELAEQK-LQQTLRKAETLPEVEAELAQ 396
Cdd:COG1842   172 EKIEEMEARAEAAAELAAGDsLDDELAELEADSEVEDELAA 212
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-403 8.10e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894    44 LEERDRLLDTLRETQETLaltQGKLHEVGHERDSLQRQLNT------ALPQEFAALTKELNVCREQLLEREEEIAELKAE 117
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRI---ENRLDELSQELSDASRKIGEiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   118 rnntrllLEHLECLVSRHERSLrmtvvkrqaqspAGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVALERCSLLEEE 195
Cdd:TIGR02169  760 -------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   196 LGATHKELMILKEQNNQKKTLTDGLLDgnheqesapstngKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASL 275
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKE-------------QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894   276 SSHAAELEEDLDTARKdliKSEEMNTKLQRE---VREAMAQKEDMEERITTLEKRYLAAQREATSVHDLnDKLENEIANK 352
Cdd:TIGR02169  888 KKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRV 963

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568952894   353 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK 403
Cdd:TIGR02169  964 EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 177-511 8.97e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDgNHEQESapstngKRSSDGSLSHEDLAKVLElqE 256
Cdd:PRK04778  102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-LYRELR------KSLLANRFSFGPALDELE--K 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  257 VIDRQAREQSQMKErLASLSSHAA------ELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKE----DMEERITTLEK 326
Cdd:PRK04778  173 QLENLEEEFSQFVE-LTESGDYVEareildQLEEELAALEQIMEEIPELLKELQTELPDQLQELKagyrELVEEGYHLDH 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  327 ryLAAQREATSVHDLNDKLENEIANKDSMHrqTEDKNRQLQERLElaeqKLQQTLRKaetlpEVEAElaQRVaalskaEE 406
Cdd:PRK04778  252 --LDIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERID----QLYDILER-----EVKAR--KYV------EK 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952894  407 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNE---EHNKRLSDTVDKLlsesnERLQLHLKERMAALEDKNSLLRE-V 482
Cdd:PRK04778  311 NSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNEselESVRQLEKQLESL-----EKQYDEITERIAEQEIAYSELQEeL 385

                         330       340       350
                  ....*....|....*....|....*....|
gi 568952894  483 ENAKKQLEETQHDKDQLVVTIEAL-KAELE 511
Cdd:PRK04778  386 EEILKQLEEIEKEQEKLSEMLQGLrKDELE 415
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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