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Conserved domains on  [gi|442626414|ref|NP_001260155|]
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Liprin-alpha, isoform E [Drosophila melanogaster]

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_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
942-1012 5.51e-44

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: 153.49  E-value: 5.51e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  942 FALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1012
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 ...
1114-1185 3.75e-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: 148.23  E-value: 3.75e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
1029-1094 2.83e-40

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: 142.61  E-value: 2.83e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 1029 MNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRL 1094
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-526 1.35e-16

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: 85.37  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG 414
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH---LKERMHALDEKNALTQELEKAR 491
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLELLAELL 469
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 442626414  492 KVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 526
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
37-408 5.74e-11

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: 67.40  E-value: 5.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAErnnt 116
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   117 rllLEHLECLVSRHERSLrmtvVKRQAA--------AQSGVSsevEVLKALKSLFEHHKALDEKVRErLRLSIEKNNMME 188
Cdd:TIGR02169  760 ---LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   189 EELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEK 268
Cdd:TIGR02169  829 EYLEKEIQELQEQR---------------------------IDLKEQIK---------SIEKEIENLNGKKEELEEELEE 872
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   349 LnEKLEQELRHKEAQL-KLHEEKIGAIEE----KLELSEQKlAQHAKLQPDmEEQLKARMEALTK 408
Cdd:TIGR02169  953 L-EDVQAELQRVEEEIrALEPVNMLAIQEyeevLKRLDELK-EKRAKLEEE-RKAILERIEEYEK 1014
 
Name Accession Description Interval E-value
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 ...
942-1012 5.51e-44

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: 153.49  E-value: 5.51e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  942 FALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1012
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 ...
1114-1185 3.75e-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: 148.23  E-value: 3.75e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
1029-1094 2.83e-40

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: 142.61  E-value: 2.83e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 1029 MNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRL 1094
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-526 1.35e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG 414
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH---LKERMHALDEKNALTQELEKAR 491
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLELLAELL 469
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 442626414  492 KVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 526
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-533 3.46e-16

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: 84.34  E-value: 3.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEE--------------ELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRI 420
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   421 RGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEEL 497
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 442626414   498 HHEKSEIMKELSKTRLEIENFKRQL--LQQEIAYNIQQ 533
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLegLEVRIDNLQER 944
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1028-1092 3.39e-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: 65.37  E-value: 3.39e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414  1028 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1092
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-530 1.92e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.02  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   43 DKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlpqEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEH 122
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-----EISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  123 LECLVSRHERSLRMTvvkrqaaaQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMmEEELSSAKEELAQYK 202
Cdd:PRK03918  250 LEGSKRKLEEKIREL--------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY-LDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  203 AGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEA----------------NELNDYAAKTHELQTII 266
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeelerlkkrltgLTPEKLEKELEELEKAK 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  267 EKQTSELSQWQRRVSDLNNKISELEENMSRVQKehckAQDQCAKLQRDLREnvaqkEDQEERITTLEKRYLNAQRESTSL 346
Cdd:PRK03918  401 EEIEEEISKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTE-----EHRKELLEEYTAELKRIEKELKEI 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  347 HDLNEKLEQELRHKEAQLKLHEE--KIGAIEEKLELSEQKLAQHAKlqpdmeEQLKARMEALTKAQERHGSAEDRIRGLE 424
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNL------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  425 TNLDEKT---NEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALT---QELEKARKVAEELH 498
Cdd:PRK03918  546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLE 625
                         490       500       510
                  ....*....|....*....|....*....|..
gi 442626414  499 HEKSEIMKELSKTRLEIENFKRQLLQQEIAYN 530
Cdd:PRK03918  626 EELDKAFEELAETEKRLEELRKELEELEKKYS 657
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
37-408 5.74e-11

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: 67.40  E-value: 5.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAErnnt 116
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   117 rllLEHLECLVSRHERSLrmtvVKRQAA--------AQSGVSsevEVLKALKSLFEHHKALDEKVRErLRLSIEKNNMME 188
Cdd:TIGR02169  760 ---LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   189 EELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEK 268
Cdd:TIGR02169  829 EYLEKEIQELQEQR---------------------------IDLKEQIK---------SIEKEIENLNGKKEELEEELEE 872
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   349 LnEKLEQELRHKEAQL-KLHEEKIGAIEE----KLELSEQKlAQHAKLQPDmEEQLKARMEALTK 408
Cdd:TIGR02169  953 L-EDVQAELQRVEEEIrALEPVNMLAIQEyeevLKRLDELK-EKRAKLEEE-RKAILERIEEYEK 1014
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-467 3.57e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA-NLPQEFATLTKELTQARETLLERDEEIGELKAERNNTR 117
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  118 LLLEHLECLVSRHERslrmtvvKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRErLRLSIEKNnmmEEELSSAKEE 197
Cdd:COG4717   160 ELEEELEELEAELAE-------LQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-LEEELEEA---QEELEELEEE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  198 LAQYKAGVVPAGVGSGSGAGS--------------AATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQ 263
Cdd:COG4717   229 LEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  264 TIIEKQTSELSQWQRRVSDL----NNKISELEENMSRVQkEHCKAQDQCAKLQRDLRENVAQKEDQE-------ERITTL 332
Cdd:COG4717   309 ALPALEELEEEELEELLAALglppDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEEL 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  333 EKRYLNAQREstslhdlnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKlaqhAKLQpDMEEQLKARMEALTKAQER 412
Cdd:COG4717   388 RAALEQAEEY--------QELKEELEELEEQLEELLGELEELLEALDEEELE----EELE-ELEEELEELEEELEELREE 454
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414  413 HGSAEDRIRGLETN--LDEKTNEVVRLNQRLKMNEEHNLRLsSTVDKLLSESNERLQ 467
Cdd:COG4717   455 LAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
30-663 6.70e-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: 57.05  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    30 NFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSlQRQINANLPQEFATltkELTQARETLLERDEEIGEL 109
Cdd:pfam15921  114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA-AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEI 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   110 KA-----ERNNTRLLLEHlECLVSRHERSLRMTVVKrqaaaqsgvsseveVLKALKSLFEHHKALDEKVRERLR-LSIEK 183
Cdd:pfam15921  190 RSilvdfEEASGKKIYEH-DSMSTMHFRSLGSAISK--------------ILRELDTEISYLKGRIFPVEDQLEaLKSES 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   184 NNMMEEELSSAKEELAQYKAgvvpagVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGvngeaNELNDYAAKTHELQ 263
Cdd:pfam15921  255 QNKIELLLQQHQDRIEQLIS------EHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR-----NQNSMYMRQLSDLE 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   264 TIIEKQTSELSQWQRRVSDlnnKISELEENMSRVQKEHCKAQ--------------DQCAKLQRDLRENVAQKEDQEERI 329
Cdd:pfam15921  324 STVSQLRSELREAKRMYED---KIEELEKQLVLANSELTEARterdqfsqesgnldDQLQKLLADLHKREKELSLEKEQN 400
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   330 TTLEKRYLNaqrESTSLHDLNEKLEQ---ELRHKEAQLKL--------HEEKIGAIEEKLELSEQKLAQHAKLQpDMEEQ 398
Cdd:pfam15921  401 KRLWDRDTG---NSITIDHLRRELDDrnmEVQRLEALLKAmksecqgqMERQMAAIQGKNESLEKVSSLTAQLE-STKEM 476
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   399 LKARMEALTKAQERHGSAEDRIRGLETNLDEK------TN-EVVRLNQRLKMNEEHNLRLSSTVDKLLSESNE----RLQ 467
Cdd:pfam15921  477 LRKVVEELTAKKMTLESSERTVSDLTASLQEKeraieaTNaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQ 556
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   468 VHLKERMHAL--DEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKrqLLQQEIAYNIQQTEALTRSLSPSS 545
Cdd:pfam15921  557 MAEKDKVIEIlrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEK 634
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   546 V--VDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALvrsmaEQEWEKLQQAAHAQQQAYE-----LASAADCDDSDVL 618
Cdd:pfam15921  635 VklVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SEDYEVLKRNFRNKSEEMEtttnkLKMQLKSAQSELE 709
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 442626414   619 YAAAT--DMMSPSGHtdAQTLAMMLQEQLDAINNEIRLIQEEKQSTE 663
Cdd:pfam15921  710 QTRNTlkSMEGSDGH--AMKVAMGMQKQITAKRGQIDALQSKIQFLE 754
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
942-1008 2.74e-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: 48.83  E-value: 2.74e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414    942 FALWNGPTIVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 1008
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1115-1185 3.32e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 48.42  E-value: 3.32e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALdeGFDANAMGlalQIPTQNAQARQILDTEFNNLL 1185
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
256-593 1.39e-06

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: 53.05  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   256 AAKTHELQTIIEKQTSELSQWQRRVSDLNNKIselEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR 335
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   336 YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGS 415
Cdd:pfam02463  225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   416 AEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSstvdKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAE 495
Cdd:pfam02463  305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   496 ELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNS-HASFETHSLRRQSKQR 574
Cdd:pfam02463  381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKL 460
                          330
                   ....*....|....*....
gi 442626414   575 LSEENALVRSMAEQEWEKL 593
Cdd:pfam02463  461 LKDELELKKSEDLLKETQL 479
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1038-1092 3.64e-06

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: 45.75  E-value: 3.64e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   1038 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
Cdd:smart00454   12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1115-1186 1.21e-04

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: 41.51  E-value: 1.21e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414   1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDanamgLALQIPTQNAQARQILDTEFNNLLQ 1186
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLKE 67
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
249-410 2.82e-04

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.28  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  249 ANELNDYAAKThelQTIIEKQTSELSQWQRRVSDLNNKiSELEENMSRVQ-------KEHCKAQDQCAKLQRDLRENVAQ 321
Cdd:cd22656    75 AGDIYNYAQNA---GGTIDSYYAEILELIDDLADATDD-EELEEAKKTIKallddllKEAKKYQDKAAKVVDKLTDFENQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  322 KEDQEERITTLEKRY------LNAQRESTSLHDLNEKLEQELRHKEAQLKlheEKIGAIEEKLELSEQKLAQHAKLQ--- 392
Cdd:cd22656   151 TEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLK---AKIDELKALIADDEAKLAAALRLIadl 227
                         170       180
                  ....*....|....*....|....*
gi 442626414  393 -------PDMEEQLKARMEALTKAQ 410
Cdd:cd22656   228 taadtdlDNLLALIGPAIPALEKLQ 252
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
945-1008 3.00e-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: 37.25  E-value: 3.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626414   945 WNGPTIVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 1008
Cdd:pfam00536    3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
PTZ00121 PTZ00121
MAEBL; Provisional
41-588 4.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  121 EHLEcLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDE--------KVRERLRLSIEKNNMMEEELS 192
Cdd:PTZ00121 1425 KKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeaKKADEAKKKAEEAKKKADEAK 1503
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  193 SAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELN--DYAAKTHELQTIIEKQT 270
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKkaEEAKKAEEDKNMALRKA 1583
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  271 SELSQWQRRVSDLNNKISELEENM----------SRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMkaeeakkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQE-RHGSAEDR 419
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDK 1743
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  420 IRGLETNLDEKTNEVVrlnQRLKMNEEhnlrlsstvdKLLSESNERLQVHLKERMHALDEKNALTQElekaRKVAEELhh 499
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKI---AHLKKEEE----------KKAEEIRKEKEAVIEEELDEEDEKRRMEVD----KKIKDIF-- 1804
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  500 EKSEIMKELSKTRLEIENFKRQLLQQEI-----AYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRqskqr 574
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIkevadSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKED----- 1879
                         570
                  ....*....|....
gi 442626414  575 lSEENALVRSMAEQ 588
Cdd:PTZ00121 1880 -DEEEIEEADEIEK 1892
 
Name Accession Description Interval E-value
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 ...
942-1012 5.51e-44

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: 153.49  E-value: 5.51e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  942 FALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 1012
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 ...
1114-1185 3.75e-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: 148.23  E-value: 3.75e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
1029-1094 2.83e-40

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: 142.61  E-value: 2.83e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414 1029 MNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRL 1094
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
949-1007 1.48e-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: 1.48e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414  949 TIVAWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1007
Cdd:cd09494     1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
1033-1092 1.98e-25

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: 100.30  E-value: 1.98e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414 1033 WIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
Cdd:cd09495     1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
1122-1183 2.69e-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: 96.84  E-value: 2.69e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1122 RVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNN 1183
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 ...
1114-1185 4.41e-24

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: 96.74  E-value: 4.41e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-526 1.35e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG 414
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH---LKERMHALDEKNALTQELEKAR 491
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLELLAELL 469
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 442626414  492 KVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQE 526
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-533 3.46e-16

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: 84.34  E-value: 3.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEE--------------ELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRI 420
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   421 RGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEEL 497
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 442626414   498 HHEKSEIMKELSKTRLEIENFKRQL--LQQEIAYNIQQ 533
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLegLEVRIDNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
255-524 4.10e-16

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: 83.95  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEK 334
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   335 RYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKArmealtkAQERHG 414
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-------LEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   415 SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqVHLKERMHALDEKNaltQELEKARKVA 494
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELE---EELEELQEEL 456
                          250       260       270
                   ....*....|....*....|....*....|
gi 442626414   495 EELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQ 486
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
1114-1185 5.65e-16

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: 73.64  E-value: 5.65e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414 1114 DVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLL 1185
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
945-1007 1.44e-15

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: 72.48  E-value: 1.44e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626414  945 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 1007
Cdd:cd09564     4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
50-683 2.69e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.14  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   50 REAQERLNETENKL-------RDVEKERDSLQRQinANLPQEFATLTKELT--QARETLLERDEeigeLKAERNNTRLLL 120
Cdd:COG1196   175 EEAERKLEATEENLerledilGELERQLEPLERQ--AEKAERYRELKEELKelEAELLLLKLRE----LEAELEELEAEL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  121 EHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALdEKVRERLRLSIEKNNMMEEELSSAKEELAQ 200
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  201 YKAgvvpagvgsgsgAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:COG1196   328 LEE------------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  281 SDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREstslhdlNEKLEQELRHK 360
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE-------EEALLELLAEL 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  361 EAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQR 440
Cdd:COG1196   469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  441 LKMNEEHNLRLSSTVDKLLSESNER---LQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 517
Cdd:COG1196   549 QNIVVEDDEVAAAAIEYLKAAKAGRatfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  518 FKRQLLQQEIAYNIQQTEALTRSLSPSSvvdpSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEKLQQAA 597
Cdd:COG1196   629 AARLEAALRRAVTLAGRLREVTLEGEGG----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  598 HAQQQAYELASAADCDDSDVLYAAATDMMspsgHTDAQTLAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESRVGSLE 677
Cdd:COG1196   705 EERELAEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780

                  ....*.
gi 442626414  678 HVNLLA 683
Cdd:COG1196   781 PVNLLA 786
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
1028-1092 1.02e-14

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: 69.75  E-value: 1.02e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1028 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
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 ...
1028-1092 1.25e-14

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: 69.65  E-value: 1.25e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414 1028 DMNHEWIGNyWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1092
Cdd:cd09566     1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
249-529 1.67e-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: 78.95  E-value: 1.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   329 ITTLEKRYLNAQREstslhdlNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTK 408
Cdd:TIGR02168  784 IEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   409 AQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLSESNERLQvhLKERMHALDEK-NALTQEL 487
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSE--LRRELEELREKlAQLELRL 931
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442626414   488 EKAR--------KVAEELHHEKSEIMKELSKTRLEIENFKRQL--LQQEIAY 529
Cdd:TIGR02168  932 EGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLkrLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
58-467 5.16e-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: 77.02  E-value: 5.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    58 ETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERslrmt 137
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAE--------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA----- 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   138 vvKRQAAAQSGVSSEVEVLKAlkslfehhkaldEKVRERLRLSIEKNnmmEEELSSAKEELAQYKAGVvpagvgsgsgag 217
Cdd:TIGR02168  741 --EVEQLEERIAQLSKELTEL------------EAEIEELEERLEEA---EEELAEAEAEIEELEAQI------------ 791
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   218 saattaggggaENGLKEKMAGVGGSGGVNGEANELNDYAaktHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRV 297
Cdd:TIGR02168  792 -----------EQLKEELKALREALDELRAELTLLNEEA---ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   298 QKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRE----STSLHDLNEKLeQELRHKEAQLKLHEEKI-- 371
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElrelESKRSELRREL-EELREKLAQLELRLEGLev 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   372 ------GAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHG----SAEDRIRGLETNLDEKTNEVVRLNQRL 441
Cdd:TIGR02168  937 ridnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQKEDLTEAK 1016
                          410       420
                   ....*....|....*....|....*.
gi 442626414   442 KmneehnlRLSSTVDKLLSESNERLQ 467
Cdd:TIGR02168 1017 E-------TLEEAIEEIDREARERFK 1035
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-464 2.41e-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: 75.09  E-value: 2.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    49 LREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKEL------------TQARETLLERDEEIGELKAERNNT 116
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQ--AEKAERYKELKAELrelelallvlrlEELREELEELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   117 RLLLEHLECLVSRHErsLRMTVVKRQAAAQSGvssEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:TIGR02168  259 TAELQELEEKLEELR--LEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   197 ELAQYKAGVVPAGVGSGSGAgsaattaggggaeNGLKEKMAGvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEEL-------------ESLEAELEE---------LEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvAQKEDQEERITTLEKrylnaqrestslhdLNEKLEQE 356
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEE--------------ELEELQEE 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   357 LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdmeeqLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVR 436
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQ-----------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          410       420       430
                   ....*....|....*....|....*....|..
gi 442626414   437 LNQRLKMNEEH----NLRLSSTVDKLLSESNE 464
Cdd:TIGR02168  525 LSELISVDEGYeaaiEAALGGRLQAVVVENLN 556
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1028-1092 3.39e-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: 65.37  E-value: 3.39e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414  1028 DMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGISMLK 1092
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-530 1.92e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.02  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   43 DKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlpqEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEH 122
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-----EISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  123 LECLVSRHERSLRMTvvkrqaaaQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMmEEELSSAKEELAQYK 202
Cdd:PRK03918  250 LEGSKRKLEEKIREL--------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY-LDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  203 AGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEA----------------NELNDYAAKTHELQTII 266
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeelerlkkrltgLTPEKLEKELEELEKAK 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  267 EKQTSELSQWQRRVSDLNNKISELEENMSRVQKehckAQDQCAKLQRDLREnvaqkEDQEERITTLEKRYLNAQRESTSL 346
Cdd:PRK03918  401 EEIEEEISKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTE-----EHRKELLEEYTAELKRIEKELKEI 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  347 HDLNEKLEQELRHKEAQLKLHEE--KIGAIEEKLELSEQKLAQHAKlqpdmeEQLKARMEALTKAQERHGSAEDRIRGLE 424
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNL------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  425 TNLDEKT---NEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALT---QELEKARKVAEELH 498
Cdd:PRK03918  546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLE 625
                         490       500       510
                  ....*....|....*....|....*....|..
gi 442626414  499 HEKSEIMKELSKTRLEIENFKRQLLQQEIAYN 530
Cdd:PRK03918  626 EELDKAFEELAETEKRLEELRKELEELEKKYS 657
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-528 6.24e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 6.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  120 LEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  200 QYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRR 279
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  280 VSDLNNK--ISELEENMSRVQKEHcKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRylNAQREStslhdlnekLEQEL 357
Cdd:COG1196   513 ALLLAGLrgLAGAVAVLIGVEAAY-EAALEAALAAALQNIVVEDDEVAAAAIEYLKAA--KAGRAT---------FLPLD 580
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARmealTKAQERHGSAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG1196   581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR----TLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  438 NQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIEN 517
Cdd:COG1196   657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
                         490
                  ....*....|.
gi 442626414  518 FKRQLLQQEIA 528
Cdd:COG1196   737 LLEELLEEEEL 747
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
157-514 2.07e-11

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: 68.54  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   157 KALKSLFEHHKALDEKVRERLRLSIEKnnmmEEELSSAKEELAQYKAGVvpagvgsgsGAGSAATTAGGGGAENGLKEKM 236
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEV---------EQLEERIAQLSKELTELEAEIE 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   237 AGVGGSGGVNGEANELndyAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLR 316
Cdd:TIGR02168  765 ELEERLEEAEEELAEA---EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   317 ENVAQKEDQEERITTLEKrylnaqrESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDME 396
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAA-------EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   397 EQLKARMEALTKAQERHGSAEDRIRGLETnldektnevvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvHLKERMHA 476
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQE----------RLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKE 983
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 442626414   477 LDEKN-ALTQELEKARKVAEELHHEKSEIMKelSKTRLE 514
Cdd:TIGR02168  984 LGPVNlAAIEEYEELKERYDFLTAQKEDLTE--AKETLE 1020
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
29-522 3.16e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.78  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   29 ANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinANLPQEFATLTKELTQARETLLERDEEIGE 108
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  109 LKAERNNTRLLLEHLECLVSRherslrmtvVKRQAAAQSGVSSEVEVLKALKSLFEHHKALD---EKVRERLR-LSIEKN 184
Cdd:PRK03918  319 LEEEINGIEERIKELEEKEER---------LEELKKKLKELEKRLEELEERHELYEEAKAKKeelERLKKRLTgLTPEKL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  185 NMMEEELSSAKEELaqykagvvpagvgsgsgagsaattaggGGAENGLKEKMAGVGGSGGVNGEA-NELNDYAAKT---- 259
Cdd:PRK03918  390 EKELEELEKAKEEI---------------------------EEEISKITARIGELKKEIKELKKAiEELKKAKGKCpvcg 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  260 -----HELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCK-----AQDQCAKLQRDLRE-----NVAQKED 324
Cdd:PRK03918  443 relteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEklkkyNLEELEK 522
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  325 QEERITTLEKRYLNAQRESTSLHDLNEKLEqELRHKEAQLklhEEKIGAIEEKLELSEQKLAqhaKLQPDMEEQLKARME 404
Cdd:PRK03918  523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL---EKKLDELEEELAELLKELE---ELGFESVEELEERLK 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  405 ALTKAQERHGSA----------EDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlRLSSTVDKLLSESNERLQVHLKERM 474
Cdd:PRK03918  596 ELEPFYNEYLELkdaekelereEKELKKLEEELDKAFEELAETEKRLEELRK---ELEELEKKYSEEEYEELREEYLELS 672
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 442626414  475 HALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:PRK03918  673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
942-1006 5.14e-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: 59.16  E-value: 5.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414  942 FALWNGPTIVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 1006
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
37-408 5.74e-11

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: 67.40  E-value: 5.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAErnnt 116
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   117 rllLEHLECLVSRHERSLrmtvVKRQAA--------AQSGVSsevEVLKALKSLFEHHKALDEKVRErLRLSIEKNNMME 188
Cdd:TIGR02169  760 ---LKELEARIEELEEDL----HKLEEAlndlearlSHSRIP---EIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   189 EELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaeNGLKEKMAgvggsggvnGEANELNDYAAKTHELQTIIEK 268
Cdd:TIGR02169  829 EYLEKEIQELQEQR---------------------------IDLKEQIK---------SIEKEIENLNGKKEELEEELEE 872
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHD 348
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS 952
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   349 LnEKLEQELRHKEAQL-KLHEEKIGAIEE----KLELSEQKlAQHAKLQPDmEEQLKARMEALTK 408
Cdd:TIGR02169  953 L-EDVQAELQRVEEEIrALEPVNMLAIQEyeevLKRLDELK-EKRAKLEEE-RKAILERIEEYEK 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-683 1.13e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   357 LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERH-------GSAEDRIRGLETNLDE 429
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   430 KTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMK 506
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   507 ELSKTRLEIENFKRQL--LQQEIAYNIQqtealtrslspssvvdpsgafsrsnshasfethslrrqskqRLSEEnalvrs 584
Cdd:TIGR02168  916 ELEELREKLAQLELRLegLEVRIDNLQE-----------------------------------------RLSEE------ 948
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   585 maeqeweklqqaahaqqqaYELAsaadcddsdvlyaaatdmmspsghtdaqtlammlqeqLDAINNEIRLIQEEKQSTEA 664
Cdd:TIGR02168  949 -------------------YSLT-------------------------------------LEEAEALENKIEDDEEEARR 972
                          410
                   ....*....|....*....
gi 442626414   665 RAEELESRVGSLEHVNLLA 683
Cdd:TIGR02168  973 RLKRLENKIKELGPVNLAA 991
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
36-497 2.83e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 64.70  E-value: 2.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   36 VSMLDERDKLMDSLREAQERLNETENKLRDVEKERdslqrqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNN 115
Cdd:PRK03918  354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEK----------LEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  116 TRLLLEHLE-----CLVSRHERS--LRMTVVKRQAAAQSGVSSEVEVLKALKslfehhkaldEKVRERLRlSIEKNNMME 188
Cdd:PRK03918  424 LKKAIEELKkakgkCPVCGRELTeeHRKELLEEYTAELKRIEKELKEIEEKE----------RKLRKELR-ELEKVLKKE 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  189 EELSSAKEELAQYKAgvvpagvgsgsgagsaattaggggaengLKEKMagvggsggvngEANELNDYAAKTHELQTIIEK 268
Cdd:PRK03918  493 SELIKLKELAEQLKE----------------------------LEEKL-----------KKYNLEELEKKAEEYEKLKEK 533
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  269 qTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE-NVAQKEDQEERITTLEKRYlnaqRESTSLH 347
Cdd:PRK03918  534 -LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFY----NEYLELK 608
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  348 DLneklEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLaqhaklqpdmeEQLKARMEALTKAqerhgSAEDRIRGLETNL 427
Cdd:PRK03918  609 DA----EKELEREEKELKKLEEELDKAFEELAETEKRL-----------EELRKELEELEKK-----YSEEEYEELREEY 668
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  428 DEKTNEVVRLNQRLKMNEEHNLRLSSTVDKllsesnerlqvhLKERMHALDEKNALTQELEKARKVAEEL 497
Cdd:PRK03918  669 LELSRELAGLRAELEELEKRREEIKKTLEK------------LKEELEEREKAKKELEKLEKALERVEEL 726
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-467 3.57e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA-NLPQEFATLTKELTQARETLLERDEEIGELKAERNNTR 117
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  118 LLLEHLECLVSRHERslrmtvvKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRErLRLSIEKNnmmEEELSSAKEE 197
Cdd:COG4717   160 ELEEELEELEAELAE-------LQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-LEEELEEA---QEELEELEEE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  198 LAQYKAGVVPAGVGSGSGAGS--------------AATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQ 263
Cdd:COG4717   229 LEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  264 TIIEKQTSELSQWQRRVSDL----NNKISELEENMSRVQkEHCKAQDQCAKLQRDLRENVAQKEDQE-------ERITTL 332
Cdd:COG4717   309 ALPALEELEEEELEELLAALglppDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEEL 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  333 EKRYLNAQREstslhdlnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKlaqhAKLQpDMEEQLKARMEALTKAQER 412
Cdd:COG4717   388 RAALEQAEEY--------QELKEELEELEEQLEELLGELEELLEALDEEELE----EELE-ELEEELEELEEELEELREE 454
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414  413 HGSAEDRIRGLETN--LDEKTNEVVRLNQRLKMNEEHNLRLsSTVDKLLSESNERLQ 467
Cdd:COG4717   455 LAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYR 510
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
40-536 4.71e-10

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: 63.89  E-value: 4.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    40 DERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLL 119
Cdd:TIGR04523  124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   120 LEHLECLVSRHeRSLRMTVVKrqaaAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELA 199
Cdd:TIGR04523  203 LSNLKKKIQKN-KSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   200 QYKAgvvpagvgsgsgagsaattaGGGGAENGLKEkmagvggsggVNGEANELNDYAAK--THELQTIIEKQ-------T 270
Cdd:TIGR04523  278 QNNK--------------------KIKELEKQLNQ----------LKSEISDLNNQKEQdwNKELKSELKNQekkleeiQ 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   271 SELSQWQRRVSDLNNKISELEE-------NMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRES 343
Cdd:TIGR04523  328 NQISQNNKIISQLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   344 TSLHDLNEKLEQELRHKEAQLKLHEEKIgaIEEKLELSEQKLAQHAKlqpdmeEQLKARMEALTKAQERHGSA-EDRIRG 422
Cdd:TIGR04523  408 QQKDEQIKKLQQEKELLEKEIERLKETI--IKNNSEIKDLTNQDSVK------ELIIKNLDNTRESLETQLKVlSRSINK 479
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   423 LETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqvhLKERMHALD-EKNALTQELE---------KARK 492
Cdd:TIGR04523  480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKEKIEKLEsEKKEKESKISdledelnkdDFEL 554
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 442626414   493 VAEELHHEKSEIMKELSKTRLEIENFKRQllQQEIAYNIQQTEA 536
Cdd:TIGR04523  555 KKENLEKEIDEKNKEIEELKQTQKSLKKK--QEEKQELIDQKEK 596
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
248-524 5.65e-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: 63.93  E-value: 5.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQdQCAKLQRDLRE-----NVAQK 322
Cdd:TIGR02169  154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyeLLKEK 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   323 EDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQL--------KLHEEKIGAIEEKLELSEQKLAQHAKLQPD 394
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnkkikDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   395 MEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK-----MN------EEHNLRLSSTVDKL----- 458
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAelkeeLEdlraelEEVDKEFAETRDELkdyre 392
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414   459 -LSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:TIGR02169  393 kLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
312-556 1.31e-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: 61.70  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  312 QRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhakL 391
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---L 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  392 QPDMEEQlKARMEALTKAQERHGSAEdrirglETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKlLSESNERLQVHLK 471
Cdd:COG4942    96 RAELEAQ-KEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAALRA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  472 ERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNiQQTEALTRSLSPSSVVDPSG 551
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTPAA 246

                  ....*
gi 442626414  552 AFSRS 556
Cdd:COG4942   247 GFAAL 251
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
250-542 3.87e-09

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: 61.19  E-value: 3.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:TIGR04523   61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNI 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   330 TTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAqhaklqpdmeeQLKARMEALTKA 409
Cdd:TIGR04523  141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-----------KLELLLSNLKKK 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   410 QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKL--LSESNERLQVHLKERMHALDEKNALTQEL 487
Cdd:TIGR04523  210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLnqLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414   488 EKARKVA----EELHHEKSE-IMKELSKtrlEIENFKRQL--LQQEIAYNIQQTEALTRSLS 542
Cdd:TIGR04523  287 EKQLNQLkseiSDLNNQKEQdWNKELKS---ELKNQEKKLeeIQNQISQNNKIISQLNEQIS 345
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
249-446 3.94e-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: 60.16  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  249 ANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  329 ITTLEKRY-------------------------LNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQ 383
Cdd:COG4942    99 LEAQKEELaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626414  384 KLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE 446
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
40-528 4.26e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.82  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   40 DERDKLMDSLREAQERLNETENK---LRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:PRK02224  227 EQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETI-AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  117 RL----LLEHLECLVSRHErSLRMTVVKRQAAAQsgvssevEVLKALKSLFEHHKALDEKVRErLRlsiEKNNMMEEELS 192
Cdd:PRK02224  306 DAdaeaVEARREELEDRDE-ELRDRLEECRVAAQ-------AHNEEAESLREDADDLEERAEE-LR---EEAAELESELE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  193 SAKEELAQYkagvvpagvgsgsgagsaattaggggaenglKEKMAGVGGSGGVNGEAneLNDYAAKTHELQTIIEKQTSE 272
Cdd:PRK02224  374 EAREAVEDR-------------------------------REEIEELEEEIEELRER--FGDAPVDLGNAEDFLEELREE 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  273 LSQWQRRVSDLNNKISELEENMSrvQKEHCKAQDQCAKLQRDLREN--VAQKEDQEERITTLEKRYLNAQRESTslhDLN 350
Cdd:PRK02224  421 RDELREREAELEATLRTARERVE--EAEALLEAGKCPECGQPVEGSphVETIEEDRERVEELEAELEDLEEEVE---EVE 495
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  351 EKLEQELRHKEAqlklhEEKIGAIEEKLELSEQKLAQH-AKLQPDME--EQLKARMEAL-TKAQERHGSAEDrirgLETN 426
Cdd:PRK02224  496 ERLERAEDLVEA-----EDRIERLEERREDLEELIAERrETIEEKREraEELRERAAELeAEAEEKREAAAE----AEEE 566
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  427 LDEKTNEVVRLNQRLKMNEE--HNLRLSSTVDKLLSESNERLQvHLKERMHALDEKNaltqelEKARKVAEELHHEKSEI 504
Cdd:PRK02224  567 AEEAREEVAELNSKLAELKEriESLERIRTLLAAIADAEDEIE-RLREKREALAELN------DERRERLAEKRERKREL 639
                         490       500
                  ....*....|....*....|....
gi 442626414  505 MKELSKTRLEIENFKRQLLQQEIA 528
Cdd:PRK02224  640 EAEFDEARIEEAREDKERAEEYLE 663
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
49-542 4.75e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.82  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   49 LREAQERLNETENKLRDVEKERDSLQRQINANLPQ-EFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLV 127
Cdd:PRK02224  164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  128 SRHERSLrmtvvkrqaaaqsgvsSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAqykagvvp 207
Cdd:PRK02224  244 EEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL-------- 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  208 agvgsgsgagsaattaggggAENGLkekmagvggsggvngEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKI 287
Cdd:PRK02224  300 --------------------AEAGL---------------DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  288 SELEENMSRVQKEHCKAQDQCAKLQ-------RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHK 360
Cdd:PRK02224  345 ESLREDADDLEERAEELREEAAELEseleearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  361 EAQLKLHEEKIGAIEEKLELSEQKLAQ--------------HAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETn 426
Cdd:PRK02224  425 REREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED- 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  427 LDEKTNEVVRLNQRLKmneehnlrlssTVDKLLSESNERLQvhlkERMHALDEKNALTQELEKArkvAEELHHEKSEIMK 506
Cdd:PRK02224  504 LVEAEDRIERLEERRE-----------DLEELIAERRETIE----EKRERAEELRERAAELEAE---AEEKREAAAEAEE 565
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 442626414  507 ELSKTRLEIENFKRQLlqQEIAYNIQQTEALTRSLS 542
Cdd:PRK02224  566 EAEEAREEVAELNSKL--AELKERIESLERIRTLLA 599
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
255-531 1.60e-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: 59.31  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   255 YAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIttlek 334
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL----- 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   335 rylnaqrestslhdlnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARMEALtkaQERH 413
Cdd:TIGR02169  747 ----------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKL---EEEV 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   414 GSAEDRIRGLETNLDEKTNEVVRLNQrlKMNEEHNLRLSSTVDKllsesnerlqVHLKERMHALD-EKNALTQELEKARK 492
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEK--EIQELQEQRIDLKEQI----------KSIEKEIENLNgKKEELEEELEELEA 875
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 442626414   493 VAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNI 531
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
251-510 1.76e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   331 TLEKrylnaqrESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQpdmeEQLKARMEALTKAQ 410
Cdd:TIGR02168  348 ELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI----ERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   411 ERhgsAEDRIRGLETNLDEKTNEVV--RLNQRLKMNEEHNLRLSSTVDKL--LSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:TIGR02168  417 ER---LQQEIEELLKKLEEAELKELqaELEELEEELEELQEELERLEEALeeLREELEEAEQALDAAERELAQLQARLDS 493
                          250       260
                   ....*....|....*....|....
gi 442626414   487 LEKARKVAEELHHEKSEIMKELSK 510
Cdd:TIGR02168  494 LERLQENLEGFSEGVKALLKNQSG 517
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
55-530 3.24e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   55 RLNETENKLRDVEkERDSLQRQI-------NA--NLpQEFATLTKELTQARETLLERDEEIGELKaeRNNTRLLLEHLec 125
Cdd:PRK03918  133 RQGEIDAILESDE-SREKVVRQIlglddyeNAykNL-GEVIKEIKRRIERLEKFIKRTENIEELI--KEKEKELEEVL-- 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  126 lvsrHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAGV 205
Cdd:PRK03918  207 ----REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  206 vpagvgsgsgagsaattAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNN 285
Cdd:PRK03918  283 -----------------KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  286 KISELEENMSRVQKEHckaqdqcaKLQRDLRENVAQKEDQEERIT-----TLEKRYLNAQRESTSLHDLNEKLEQ---EL 357
Cdd:PRK03918  346 KLKELEKRLEELEERH--------ELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITArigEL 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLqpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLD---EKTNEV 434
Cdd:PRK03918  418 KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESEL 495
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  435 VRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvHLKERMHAL-----------DEKNALTQELEKARKVAEELHHEKSE 503
Cdd:PRK03918  496 IKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLkgeikslkkelEKLEELKKKLAELEKKLDELEEELAE 574
                         490       500
                  ....*....|....*....|....*...
gi 442626414  504 IMKELSKTRLE-IENFKRQLLQQEIAYN 530
Cdd:PRK03918  575 LLKELEELGFEsVEELEERLKELEPFYN 602
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
326-473 4.18e-08

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: 55.32  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  326 EERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKlqpdmEEQLKARMEA 405
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----NKEYEALQKE 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414  406 LTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKER 473
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
30-663 6.70e-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: 57.05  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    30 NFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSlQRQINANLPQEFATltkELTQARETLLERDEEIGEL 109
Cdd:pfam15921  114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA-AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEI 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   110 KA-----ERNNTRLLLEHlECLVSRHERSLRMTVVKrqaaaqsgvsseveVLKALKSLFEHHKALDEKVRERLR-LSIEK 183
Cdd:pfam15921  190 RSilvdfEEASGKKIYEH-DSMSTMHFRSLGSAISK--------------ILRELDTEISYLKGRIFPVEDQLEaLKSES 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   184 NNMMEEELSSAKEELAQYKAgvvpagVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGvngeaNELNDYAAKTHELQ 263
Cdd:pfam15921  255 QNKIELLLQQHQDRIEQLIS------EHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR-----NQNSMYMRQLSDLE 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   264 TIIEKQTSELSQWQRRVSDlnnKISELEENMSRVQKEHCKAQ--------------DQCAKLQRDLRENVAQKEDQEERI 329
Cdd:pfam15921  324 STVSQLRSELREAKRMYED---KIEELEKQLVLANSELTEARterdqfsqesgnldDQLQKLLADLHKREKELSLEKEQN 400
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   330 TTLEKRYLNaqrESTSLHDLNEKLEQ---ELRHKEAQLKL--------HEEKIGAIEEKLELSEQKLAQHAKLQpDMEEQ 398
Cdd:pfam15921  401 KRLWDRDTG---NSITIDHLRRELDDrnmEVQRLEALLKAmksecqgqMERQMAAIQGKNESLEKVSSLTAQLE-STKEM 476
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   399 LKARMEALTKAQERHGSAEDRIRGLETNLDEK------TN-EVVRLNQRLKMNEEHNLRLSSTVDKLLSESNE----RLQ 467
Cdd:pfam15921  477 LRKVVEELTAKKMTLESSERTVSDLTASLQEKeraieaTNaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealKLQ 556
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   468 VHLKERMHAL--DEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKrqLLQQEIAYNIQQTEALTRSLSPSS 545
Cdd:pfam15921  557 MAEKDKVIEIlrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEK 634
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   546 V--VDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALvrsmaEQEWEKLQQAAHAQQQAYE-----LASAADCDDSDVL 618
Cdd:pfam15921  635 VklVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SEDYEVLKRNFRNKSEEMEtttnkLKMQLKSAQSELE 709
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 442626414   619 YAAAT--DMMSPSGHtdAQTLAMMLQEQLDAINNEIRLIQEEKQSTE 663
Cdd:pfam15921  710 QTRNTlkSMEGSDGH--AMKVAMGMQKQITAKRGQIDALQSKIQFLE 754
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-677 6.78e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   257 AKTHELQTIIEkQTSELSQWQRRVSDLNNKISELEENMSRV---------QKEHCKAQDQCAKLQRDLREnvaQKEDQEE 327
Cdd:TIGR02168  152 AKPEERRAIFE-EAAGISKYKERRKETERKLERTRENLDRLedilnelerQLKSLERQAEKAERYKELKA---ELRELEL 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   328 RITTLEkrylnaqrestsLHDLNEKLEQelrhKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLkarmealT 407
Cdd:TIGR02168  228 ALLVLR------------LEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-------E 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   408 KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKL---LSESNERLQVhLKERMHALDEKNAlt 484
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEE-LKEELESLEAELE-- 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   485 qELEKARKVAEELHHEKSEIMKELSKTRLEIENfKRQLLQQEIAYNIQQTEALTRSLspssvvdpsgafsrsnshasfet 564
Cdd:TIGR02168  362 -ELEAELEELESRLEELEEQLETLRSKVAQLEL-QIASLNNEIERLEARLERLEDRR----------------------- 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   565 hslrrqskQRLSEENALVRsMAEQEWEKLQQAAHAQQQAYELASAADCDDSdvlyaaatdmmspsghtdaqtlammLQEQ 644
Cdd:TIGR02168  417 --------ERLQQEIEELL-KKLEEAELKELQAELEELEEELEELQEELER-------------------------LEEA 462
                          410       420       430
                   ....*....|....*....|....*....|...
gi 442626414   645 LDAINNEIRLIQEEKQSTEARAEELESRVGSLE 677
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLE 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
19-427 9.76e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   19 QRSSQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARET 98
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEE 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   99 LLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEhhKALDEKVRERLR 178
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE--AALEAALAAALQ 549
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  179 LSIEKNnmmEEELSSAKEELAQYKAGVVpagvgsgsgagsAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAK 258
Cdd:COG1196   550 NIVVED---DEVAAAAIEYLKAAKAGRA------------TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  259 THELQTIIEKQTSE---LSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERittLEKR 335
Cdd:COG1196   615 YYVLGDTLLGRTLVaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER---LAEE 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  336 YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGS 415
Cdd:COG1196   692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
                         410
                  ....*....|...
gi 442626414  416 AEDRIRGLET-NL 427
Cdd:COG1196   772 LEREIEALGPvNL 784
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
44-678 1.24e-07

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: 56.13  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    44 KLMDSLREAQERLNETENKLRDVEK---ERDSLQRQINANLP--QEFATLTKELTQARETL------------LERDEEI 106
Cdd:TIGR00618  226 KELKHLREALQQTQQSHAYLTQKREaqeEQLKKQQLLKQLRAriEELRAQEAVLEETQERInrarkaaplaahIKAVTQI 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   107 gELKAERNNTRLllehleclvSRHERSLRMTVVKRQAAAQSGVSSEvEVLKALKSLFEHHkaldekvrERLRLSIEKNNM 186
Cdd:TIGR00618  306 -EQQAQRIHTEL---------QSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQE--------IHIRDAHEVATS 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   187 MEEELSSAKEELAQYKAgvvpagvgsgsgagSAATTAGGGGAENGLKEKMagvggsggvngeanelndyaAKTHELQTII 266
Cdd:TIGR00618  367 IREISCQQHTLTQHIHT--------------LQQQKTTLTQKLQSLCKEL--------------------DILQREQATI 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   267 EKQTSELSQWQRRVSDLNNKIsELEENMSRVQKEHCKAQDQCAKL----QRDLRENVAQKEDQEERITTLEKRYlnAQRE 342
Cdd:TIGR00618  413 DTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLekihLQESAQSLKEREQQLQTKEQIHLQE--TRKK 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   343 STSLHDLNEKLEQELRHKEAQLKLHEEKI-----GAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAE 417
Cdd:TIGR00618  490 AVVLARLLELQEEPCPLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   418 D-------RIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERL---QVHLKERMHALDEKNALTQEL 487
Cdd:TIGR00618  570 QsfsiltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqDVRLHLQQCSQELALKLTALH 649
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   488 EKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLS-PSSVVDPSGAFSRSNSHASFETHS 566
Cdd:TIGR00618  650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTlLRELETHIEEYDREFNEIENASSS 729
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   567 LRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASAADCDDSDVLYAAAT-----DMMSPSGHTDAQTLAMML 641
Cdd:TIGR00618  730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEiqffnRLREEDTHLLKTLEAEIG 809
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 442626414   642 Q---EQLDAINNEIRLIQEEKQSTEARAEELESRVGSLEH 678
Cdd:TIGR00618  810 QeipSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
248-440 1.75e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  248 EANELNDYAAKTHELQTIIEKQTSELSQW--QRRVSDLNNKISELEEnmsrvqkehckaqdQCAKLQRDLRENVAQKEDQ 325
Cdd:COG4913   256 PIRELAERYAAARERLAELEYLRAALRLWfaQRRLELLEAELEELRA--------------ELARLEAELERLEARLDAL 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  326 EERITTLEKRYLNAQ-RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARME 404
Cdd:COG4913   322 REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 442626414  405 ALtkaQERHGSAEDRIRGLETNLDEKTNEVVRLNQR 440
Cdd:COG4913   402 AL---EEALAEAEAALRDLRRELRELEAEIASLERR 434
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
942-1008 2.74e-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: 48.83  E-value: 2.74e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414    942 FALWNGPTIVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 1008
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
37-474 2.76e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQI------NANLPQEFATLTKELTQARETLLER-------D 103
Cdd:PRK02224  311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleerAEELREEAAELESELEEAREAVEDRreeieelE 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  104 EEIGELKAERNNTRLLLE----HLECLVSRHERslrmtVVKRQAAAQSGVSSEVEVLKALKSLFE--------------- 164
Cdd:PRK02224  391 EEIEELRERFGDAPVDLGnaedFLEELREERDE-----LREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsp 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  165 HHKALDEKVRERLRLSIEKNNmMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagVGGSGG 244
Cdd:PRK02224  466 HVETIEEDRERVEELEAELED-LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK---RERAEE 541
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  245 VNGEANELNDYAAKTHELQTiieKQTSELSQWQRRVSDLNNKISELEENMSRVqkehckaqdqcaklqRDLRENVAQKED 324
Cdd:PRK02224  542 LRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELKERIESL---------------ERIRTLLAAIAD 603
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  325 QEERITTL-EKRYLNAQRESTSLHDLNEKLEqelRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARM 403
Cdd:PRK02224  604 AEDEIERLrEKREALAELNDERRERLAEKRE---RKRELEAEFDEARIEEAREDKERAEEYLEQ-------VEEKLDELR 673
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  404 EALTKAQERHGSAEDRIRGLEtNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERlQVHLKERM 474
Cdd:PRK02224  674 EERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGDLRAELRQR-NVETLERM 742
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-492 3.23e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  121 EHLEclvsRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQ 200
Cdd:COG1196   403 EELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  201 YKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELND-----YAAKTHELQTIIEKQTSELSQ 275
Cdd:COG1196   479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVeaayeAALEAALAAALQNIVVEDDEV 558
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  276 WQRRVSDLNNK----ISELEENMSRVQKEHCKAQDQCAKLQRdlRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNE 351
Cdd:COG1196   559 AAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAA--VDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  352 KLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERhgsAEDRIRGLETNLDEKT 431
Cdd:COG1196   637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE---ALLAEEEEERELAEAE 713
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  432 NEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARK 492
Cdd:COG1196   714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1115-1185 3.32e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 48.42  E-value: 3.32e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626414  1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALdeGFDANAMGlalQIPTQNAQARQILDTEFNNLL 1185
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-515 5.36e-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: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  287 ISELEENM---SRVQKEHCKAQDQCAKLQ------RDLRENVAQKEDQEERITTLekRYLNAQRESTSLHDLNEKLEQEL 357
Cdd:COG4913   227 ADALVEHFddlERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  358 RHKEAQLKLHEEKIGAIEEKLELSEQKLAQH--AKLQpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVV 435
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  436 RLNQRLKmneehnlRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELE--KARK--VAEELHHEKSEIMKELSKT 511
Cdd:COG4913   384 ALRAEAA-------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKsnIPARLLALRDALAEALGLD 456

                  ....
gi 442626414  512 RLEI 515
Cdd:COG4913   457 EAEL 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
93-424 5.66e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 5.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    93 TQARETLLERDEEIGELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAAAqsgVSSEVEVLKAlkslfEHhkaldEK 172
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKIGE---IEKEIEQLEQ-----EE-----EK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   173 VRERLRLSIEKNNMMEEELSSAKEELAQYkAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAgvggsggvngEANEL 252
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA----------ELSKL 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   253 NDYAAK----THELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR02169  804 EEEVSRiearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   329 ITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhakLQPDMEEQLKARmealtK 408
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE---DEEIPEEELSLE-----D 955
                          330
                   ....*....|....*.
gi 442626414   409 AQERHGSAEDRIRGLE 424
Cdd:TIGR02169  956 VQAELQRVEEEIRALE 971
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
261-421 6.19e-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: 51.85  E-value: 6.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  261 ELQTIIEKQT--SELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR--- 335
Cdd:COG1579     5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgn 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  336 ------YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQH--------AKLQPDMEEQLKA 401
Cdd:COG1579    85 vrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKkaeldeelAELEAELEELEAE 164
                         170       180
                  ....*....|....*....|
gi 442626414  402 RMEALTKAQERHGSAEDRIR 421
Cdd:COG1579   165 REELAAKIPPELLALYERIR 184
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
19-522 9.09e-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: 53.49  E-value: 9.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    19 QRSSQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANlpqefatlTKELTQARET 98
Cdd:TIGR04523  211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK--------QKELEQNNKK 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    99 LLERDEEIGELKAErnntrllLEHLeclvsrherslrmtvvKRQAAAqsgvssevEVLKALKSLFEHHKaldEKVRErLR 178
Cdd:TIGR04523  283 IKELEKQLNQLKSE-------ISDL----------------NNQKEQ--------DWNKELKSELKNQE---KKLEE-IQ 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   179 LSIEKNNmmeEELSSAKEELAQYKagvvpagvgsgsgagsaattaggggaenglKEKMAGVGGSGGVNGEANElndyaaK 258
Cdd:TIGR04523  328 NQISQNN---KIISQLNEQISQLK------------------------------KELTNSESENSEKQRELEE------K 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   259 THELQTIIEKQTS---ELSQWQRRVSDLNNKIS-------ELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEER 328
Cdd:TIGR04523  369 QNEIEKLKKENQSykqEIKNLESQINDLESKIQnqeklnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   329 ITTLEKRY--LNAQRES--TSLHDLN---EKLEQELRHKEAQLKLHEEKIGAI-EEKLELSEQ--KLAQHAKLQPDMEEQ 398
Cdd:TIGR04523  449 DSVKELIIknLDNTRESleTQLKVLSrsiNKIKQNLEQKQKELKSKEKELKKLnEEKKELEEKvkDLTKKISSLKEKIEK 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   399 LKArmEALTKAQERhGSAEDRI---------RGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNErlqvh 469
Cdd:TIGR04523  529 LES--EKKEKESKI-SDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD----- 600
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442626414   470 LKERMHALDEKNA-LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:TIGR04523  601 LIKEIEEKEKKISsLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
PTZ00121 PTZ00121
MAEBL; Provisional
40-507 1.11e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   40 DERDKLMDSLREAQE--RLNETENKLRDVEKERDSLQRQinANLPQEFATLTKELTQARETLLERDEEigELKAERNNTR 117
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKKK--AEEAKKAAEAAKAEAEAAADEAEAAEE--KAEAAEKKKE 1374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  118 LLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVR--ERLRLSIEKNNMMEEELSSAK 195
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAE 1454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  196 E----ELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELN--DYAAKTHELQTIIEKQ 269
Cdd:PTZ00121 1455 EakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAKKADEAKKAEEAK 1534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  270 TSElsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRD----LRENVAQKEDQEERITTLEKRYlnaqRESTS 345
Cdd:PTZ00121 1535 KAD----EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmaLRKAEEAKKAEEARIEEVMKLY----EEEKK 1606
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  346 LHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDmEEQLKARMEALTKAQERHG-------SAED 418
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKkkaeeakKAEE 1685
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  419 RIRGLETNLDEKTNEVVRLNQRLKMNEE-----HNLRLSSTVDKLLSESNERLQVHLKERMHAL----DEKNALTQELEK 489
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEekkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeEEKKKIAHLKKE 1765
                         490
                  ....*....|....*...
gi 442626414  490 ARKVAEELHHEKSEIMKE 507
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEE 1783
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
256-593 1.39e-06

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: 53.05  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   256 AAKTHELQTIIEKQTSELSQWQRRVSDLNNKIselEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR 335
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   336 YLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGS 415
Cdd:pfam02463  225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   416 AEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSstvdKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAE 495
Cdd:pfam02463  305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   496 ELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNS-HASFETHSLRRQSKQR 574
Cdd:pfam02463  381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKL 460
                          330
                   ....*....|....*....
gi 442626414   575 LSEENALVRSMAEQEWEKL 593
Cdd:pfam02463  461 LKDELELKKSEDLLKETQL 479
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
17-592 1.92e-06

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: 52.36  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    17 ISQRSSQFSGEDANFeQLMVSMLDERDKLMDSLREAQERLNETENKLRD--VEKERDSLQRQINANLPQEFATLTKELTQ 94
Cdd:TIGR00606  338 LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLIQSLATRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTAAQLCAD 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    95 ARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSgvssevevlkaLKSLFEHHKALDEKVR 174
Cdd:TIGR00606  417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS-----------SDRILELDQELRKAER 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   175 ErlrLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGS-----GGVNGEA 249
Cdd:TIGR00606  486 E---LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkikSRHSDEL 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQEERI 329
Cdd:TIGR00606  563 TSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-VCGSQDEESDL 641
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   330 TTLEKRYLNAQRESTSLH---DLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:TIGR00606  642 ERLKEEIEKSSKQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   407 TKAQER-------HGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN---------ERLQVHL 470
Cdd:TIGR00606  722 EKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMEL 801
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   471 KERMHALDEKNALTQELEKARKVaEELHHEKSEIMKELSKTRLEIE-NFKRQLLQQEIAYNIQQT--EALTRSLSPSSVV 547
Cdd:TIGR00606  802 KDVERKIAQQAAKLQGSDLDRTV-QQVNQEKQEKQHELDTVVSKIElNRKLIQDQQEQIQHLKSKtnELKSEKLQIGTNL 880
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 442626414   548 DPSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEK 592
Cdd:TIGR00606  881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
262-677 2.31e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   262 LQTIIEKQTSELSQwqrRVSDLNNKISELEENMSRVQKEhckAQDQCAKLQRDLRENVAQK-EDQEERITTLEKRYLNAQ 340
Cdd:pfam15921  218 LGSAISKILRELDT---EISYLKGRIFPVEDQLEALKSE---SQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSAR 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKL--ELSEQKLAQHAKLQpDMEEQLKARMEALTKAQ-------E 411
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLrsELREAKRMYEDKIE-ELEKQLVLANSELTEARterdqfsQ 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   412 RHGSAEDRIRGLETNLDEKTNEvvrlnqrLKMNEEHNLRL-------SSTVDKLLSESNER-----------------LQ 467
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKE-------LSLEKEQNKRLwdrdtgnSITIDHLRRELDDRnmevqrleallkamkseCQ 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   468 VHLKERMHALDEKNaltQELEKARKVAEELHHEKS---EIMKELSKTRLEIENFKRQLlqQEIAYNIQQTEaltRSLSPS 544
Cdd:pfam15921  444 GQMERQMAAIQGKN---ESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTV--SDLTASLQEKE---RAIEAT 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   545 SVvDPSGAFSRSNshasfethsLRRQSKQRLSEENALVRSmAEQEWEKLQQAAHAQQQAYElasaadcddsdVLYAAATD 624
Cdd:pfam15921  516 NA-EITKLRSRVD---------LKLQELQHLKNEGDHLRN-VQTECEALKLQMAEKDKVIE-----------ILRQQIEN 573
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414   625 MMSPSGHTDAQTLAMMLQE-QLDAINNEIRLIQEE----KQSTEARAEELESRVGSLE 677
Cdd:pfam15921  574 MTQLVGQHGRTAGAMQVEKaQLEKEINDRRLELQEfkilKDKKDAKIRELEARVSDLE 631
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
287-534 2.49e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  287 ISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQREStslhdlnEKLEQELRHKEAQLKL 366
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELNEQLQAAQAELAQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  367 HEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE 446
Cdd:COG4372    99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  447 HNLRlsSTVDKLLSESNERLQVH--LKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQ 524
Cdd:COG4372   179 AEAE--QALDELLKEANRNAEKEeeLAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
                         250
                  ....*....|
gi 442626414  525 QEIAYNIQQT 534
Cdd:COG4372   257 LKEIEELELA 266
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
32-489 2.53e-06

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: 51.75  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINaNLPQ-------EFATLTKELTQARETLLERDE 104
Cdd:pfam10174  337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR-DLKDmldvkerKINVLQKKIENLQEQLRDKDK 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   105 EIGELK-------AERNNTRLLLEHLECLVSRHERslrmtvvkrqaaaqsgvsseveVLKALKslfEHHKALDEKVRERL 177
Cdd:pfam10174  416 QLAGLKervkslqTDSSNTDTALTTLEEALSEKER----------------------IIERLK---EQREREDRERLEEL 470
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   178 RLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKmagvggsggVNGEANELNDYAA 257
Cdd:pfam10174  471 ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQ---------KKEECSKLENQLK 541
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   258 KTHELQTIiekqtselsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYL 337
Cdd:pfam10174  542 KAHNAEEA-----------VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTL 610
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   338 NAQRESTSLHDLNEKLEQELRHKEAQLklheekigaIEEKLELSEQKLAQHAKLQpdMEEQlkarMEALTKAQERHGSAE 417
Cdd:pfam10174  611 RQMKEQNKKVANIKHGQQEMKKKGAQL---------LEEARRREDNLADNSQQLQ--LEEL----MGALEKTRQELDATK 675
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   418 DRIRGLETNLDEKTNEVVRLNQ--------RLKMNEEHNLRLSSTVDK---LLSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:pfam10174  676 ARLSSTQQSLAEKDGHLTNLRAerrkqleeILEMKQEALLAAISEKDAniaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755

                   ...
gi 442626414   487 LEK 489
Cdd:pfam10174  756 LKQ 758
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-464 3.32e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   331 TLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARMEALTKAQ 410
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK-------QEWKLEQLAADLSKYE 468
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442626414   411 ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNlRLSSTVDKLLSESNE 464
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV-RGGRAVEEVLKASIQ 521
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
251-406 3.55e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaQDQcAKLQRDLRENVAQKEDQEERIT 330
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGN-VRNNKEYEALQKEIESLKRRIS 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414  331 TLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKL-AQHAKLQPDMEEQLKARMEAL 406
Cdd:COG1579   107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERI 183
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1038-1092 3.64e-06

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: 45.75  E-value: 3.64e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   1038 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLK 1092
Cdd:smart00454   12 WLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
42-536 3.83e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   42 RDKLMDSLREAQERL-NETENKLRDVEKERDSLQRQInanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:COG4717    44 RAMLLERLEKEADELfKPQGRKPELNLKELKELEEEL-----KEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  121 EHLECLVSRHERSLRMTVVKRQaaaqsgvssevevlkaLKSLFEHHKALDEKVRERLRLsieknnmmEEELSSAKEELAQ 200
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAE----------------LAELPERLEELEERLEELREL--------EEELEELEAELAE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  201 ykagvvpagvgsgsgagsaattaggggaengLKEKMAGVGGSGGVNGEaNELNDYAAKTHELQTIIEKQTSELSQWQRRV 280
Cdd:COG4717   175 -------------------------------LQEELEELLEQLSLATE-EELQDLAEELEELQQRLAELEEELEEAQEEL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  281 SDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDqeeRITTLEKRYLNAQRESTSL-----------HDL 349
Cdd:COG4717   223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG---SLLSLILTIAGVLFLVLGLlallflllareKAS 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  350 NEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERH--GSAEDRIRGLETNL 427
Cdd:COG4717   300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEA 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  428 DEKTNEvvRLNQRLKMNEE-HNLRlsstvdKLLSESNERLQVHLKERMHALD--EKNALTQELEKARKVAEELHHEKSEI 504
Cdd:COG4717   380 GVEDEE--ELRAALEQAEEyQELK------EELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEEL 451
                         490       500       510
                  ....*....|....*....|....*....|..
gi 442626414  505 MKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG4717   452 REELAELEAELEQLEEDGELAELLQELEELKA 483
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
263-439 5.22e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 5.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  263 QTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKR------- 335
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  336 ---------YLNAQRESTSLHDLNEKLE----------QELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDME 396
Cdd:COG3883    95 lyrsggsvsYLDVLLGSESFSDFLDRLSalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 442626414  397 EQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQ 439
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
229-522 5.71e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   229 ENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQwqrRVSDLNNKISELEENMS--RVQKE------ 300
Cdd:pfam05483  137 EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQ---VYMDLNNNIEKMILAFEelRVQAEnarlem 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   301 HCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEK--- 377
Cdd:pfam05483  214 HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdh 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   378 ----LELSEQKLAQHAKLQPDMEEQLK--------------ARMEALTKAQERHGSAEDRIRGLETNLDE--KTNEvvrl 437
Cdd:pfam05483  294 ltkeLEDIKMSLQRSMSTQKALEEDLQiatkticqlteekeAQMEELNKAKAAHSFVVTEFEATTCSLEEllRTEQ---- 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   438 nQRLKMNEEHNLRLSSTVDKLLSESNERL------QVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKT 511
Cdd:pfam05483  370 -QRLEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
                          330
                   ....*....|.
gi 442626414   512 RLEIENFKRQL 522
Cdd:pfam05483  449 EKEIHDLEIQL 459
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
272-536 5.98e-06

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: 50.72  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  272 ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE-NVAQKEDQEERITTLEKRYLNAQrestslhdln 350
Cdd:COG3096   837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQaNLLADETLADRLEELREELDAAQ---------- 906
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  351 ekleqelrhkEAQ--LKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEE------QLKARMEALTKAQER--HGSAEDRI 420
Cdd:COG3096   907 ----------EAQafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQakeqqrRLKQQIFALSEVVQRrpHFSYEDAV 976
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  421 RGLETNLDekTNEvvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQV--HLKERMHA-LDEKNALTQEL---------- 487
Cdd:COG3096   977 GLLGENSD--LNE--KLRARLEQAEEARREAREQLRQAQAQYSQYNQVlaSLKSSRDAkQQTLQELEQELeelgvqadae 1052
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414  488 --EKARKVAEELHHE-------KSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG3096  1053 aeERARIRRDELHEElsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
12-516 8.85e-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: 50.22  E-value: 8.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    12 ISEDSISQRSSQFSGEDANF----EQLMVSMLDERDKLmDSLREAQERLNETENKLRDVEKERDSLQRQInANLPQEFAT 87
Cdd:pfam12128  206 LEDDGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRPEF-TKLQQEFNTLESAELRLSHLHFGYKSDETLI-ASRQEERQE 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    88 LTKELTQARETLLE-----RDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQS--GVSSEVEVL-KAL 159
Cdd:pfam12128  284 TSAELNQLLRTLDDqwkekRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQlpSWQSELENLeERL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   160 KSLFEHHKALDEKVRERLRLSIEKNNmmeEELSSAKEELAQYKAGVVpagvgsgsgAGSAATTAGGGGAENGLKEKMAGV 239
Cdd:pfam12128  364 KALTGKHQDVTAKYNRRRSKIKEQNN---RDIAGIKDKLAKIREARD---------RQLAVAEDDLQALESELREQLEAG 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   240 GGSGGVNGEANELNDYAAKTHELQTIIEKQTselsqwqrrVSDLNNKISELEenmsRVQKEHCKAQDQCAKLQRDLRENV 319
Cdd:pfam12128  432 KLEFNEEEYRLKSRLGELKLRLNQATATPEL---------LLQLENFDERIE----RAREEQEAANAEVERLQSELRQAR 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   320 AQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRH---KEAQL-----------------KLHEEKIGA-IEEKL 378
Cdd:pfam12128  499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHflrKEAPDweqsigkvispellhrtDLDPEVWDGsVGGEL 578
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   379 ELSEQKLAQHAKLQPD---MEEQLKARM----EALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRL 451
Cdd:pfam12128  579 NLYGVKLDLKRIDVPEwaaSEEELRERLdkaeEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL 658
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414   452 SSTVDKLLSESNERLQVHLK---ERMHALD-EKNALTQELEKARkvaEELHHEKSEIMKELSKTRLEIE 516
Cdd:pfam12128  659 FDEKQSEKDKKNKALAERKDsanERLNSLEaQLKQLDKKHQAWL---EEQKEQKREARTEKQAYWQVVE 724
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1038-1088 9.93e-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: 44.15  E-value: 9.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442626414 1038 WLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGI 1088
Cdd:cd09487     5 WLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
151-535 1.04e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   151 SEVEVLKALKSLFEHHKALDEKVRErlrlsiEKNNMMEEE-LSSAKEELAQykagvvpagvgsgsgagsaaTTAGGGGAE 229
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQ------EKFEKMEQErLRQEKEEKAR--------------------EVERRRKLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   230 NGLKEKMAGVGGSGGVNGEANELNdyAAKTHELQTI-IEKQTSELSQWqrRVSDLNNKISELEEnMSRVQKEHckaQDQC 308
Cdd:pfam17380  320 EAEKARQAEMDRQAAIYAEQERMA--MERERELERIrQEERKRELERI--RQEEIAMEISRMRE-LERLQMER---QQKN 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   309 AKLQRDLRENVAQKEDQEERittlEKRYLNAQRESTSLhdlneKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQH 388
Cdd:pfam17380  392 ERVRQELEAARKVKILEEER----QRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   389 AKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKtnevvrlnqRLKMNEEHNLRlsstvdKLLSESNERLQ- 467
Cdd:pfam17380  463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER---------KQAMIEEERKR------KLLEKEMEERQk 527
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414   468 -VHLKERMHALDEKNALTQELEKARKVAEELHHEKSEimkelsKTRLEIENFKRQLLQQEIAYNIQQTE 535
Cdd:pfam17380  528 aIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE------RSRLEAMEREREMMRQIVESEKARAE 590
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
251-433 1.17e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREnvaQKEDQEERIT 330
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERAR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  331 TLEKR-----YLNAQRESTSLHDLNEK---LEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKAR 402
Cdd:COG3883    94 ALYRSggsvsYLDVLLGSESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442626414  403 MEALTKAQERHGSAEDRIRGLETNLDEKTNE 433
Cdd:COG3883   174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
PTZ00121 PTZ00121
MAEBL; Provisional
49-539 1.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   49 LREAQErLNETENKLRDVEKERDSLQRQINANLPQEFATLTKELTQARETLlERDEEIGELKAERNNTRLLLEHLECLVS 128
Cdd:PTZ00121 1187 VRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK-KDAEEAKKAEEERNNEEIRKFEEARMAH 1264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  129 RHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVR-ERLRLSIEKNNMMEEelSSAKEELAQYKAgvvp 207
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEE--AKKKADAAKKKA---- 1338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  208 AGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAA---KTHELQTIIEKQTSELSQWQRRVSDlN 284
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAA-K 1417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  285 NKISELEENMSRVQK--------EHCKAQDQCAKLQRDLR--ENVAQKEDQEERITTLEKRYLNAQR--ESTSLHDLNEK 352
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKK 1497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  353 LEQELRHKEAQLKLHEEKIGAiEEKLELSEQKLAQHAKLQPDM---EEQLKA----------RMEALTKAQERHGSAEDR 419
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKA-EEAKKADEAKKAEEAKKADEAkkaEEKKKAdelkkaeelkKAEEKKKAEEAKKAEEDK 1576
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  420 IRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN--ERLQVHLKERMHALDEKNALTQELEKARKVAEEl 497
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA- 1655
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 442626414  498 hHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTR 539
Cdd:PTZ00121 1656 -EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
PRK12704 PRK12704
phosphodiesterase; Provisional
365-535 3.00e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  365 KLHEEKIGAIEEKLElseqKLAQHAKLQpdMEEQLKarmEALTKAQERhgsAEDRIRGLETNLDEKTNEVVRLNQRLKMN 444
Cdd:PRK12704   27 KIAEAKIKEAEEEAK----RILEEAKKE--AEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  445 EEhnlrlssTVDKLLsESNERLQVHLKERMHALDEKnalTQELEKARKVAEELHHEKSEIMKELSKtrLEIENFKRQLLQ 524
Cdd:PRK12704   95 EE-------NLDRKL-ELLEKREEELEKKEKELEQK---QQELEKKEEELEELIEEQLQELERISG--LTAEEAKEILLE 161
                         170
                  ....*....|....*...
gi 442626414  525 Q-------EIAYNIQQTE 535
Cdd:PRK12704  162 KveeearhEAAVLIKEIE 179
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
50-203 3.05e-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: 46.84  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   50 REAQERLNEtenkLRDVEKERDSLQRQInANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSR 129
Cdd:COG1579     3 PEDLRALLD----LQELDSELDRLEHRL-KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414  130 HERSLRMTVVKRQAAAqsgVSSEVEVLKALKSLFEHH-KALDEKVrERLRLSIEKnnmMEEELSSAKEELAQYKA 203
Cdd:COG1579    78 YEEQLGNVRNNKEYEA---LQKEIESLKRRISDLEDEiLELMERI-EELEEELAE---LEAELAELEAELEEKKA 145
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
174-489 3.11e-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: 48.43  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   174 RERLRLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGL------KEKMAGVGGSGGVNG 247
Cdd:pfam02463  197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskqeieKEEEKLAQVLKENKE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:pfam02463  277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   328 RITTLEKRYLNA----QRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKlaqhaklqpdmEEQLKARM 403
Cdd:pfam02463  357 EEEELEKLQEKLeqleEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL-----------EDLLKEEK 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   404 EALTKAQErhgSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSstvDKLLSESNERLQVHLKERMHALDEKNAL 483
Cdd:pfam02463  426 KEELEILE---EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE---DLLKETQLVKLQEQLELLLSRQKLEERS 499

                   ....*.
gi 442626414   484 TQELEK 489
Cdd:pfam02463  500 QKESKA 505
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
284-526 4.40e-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: 47.71  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   284 NNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQ 363
Cdd:TIGR04523   32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   364 LKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKM 443
Cdd:TIGR04523  112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   444 --NEEHNLRLSSTVDKLLSESNERLQ---VHLKERMHAL--------DEKNALTQELEKARKVAEELHHEKSEIMKELSK 510
Cdd:TIGR04523  192 ikNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLkdniekkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
                          250
                   ....*....|....*.
gi 442626414   511 TRLEIENFKRQLLQQE 526
Cdd:TIGR04523  272 KQKELEQNNKKIKELE 287
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
266-542 4.43e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQR---- 341
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEelee 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  342 ---ESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARMEALTK-AQERHGSA 416
Cdd:COG4372   120 lqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALDELLKeANRNAEKE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  417 EDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMH--------ALDEKNALTQELE 488
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKeieelelaILVEKDTEEEELE 279
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442626414  489 KARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLS 542
Cdd:COG4372   280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
PRK11281 PRK11281
mechanosensitive channel MscK;
261-477 4.80e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN-VAQKEDQEERITTL--EKRYL 337
Cdd:PRK11281  125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGkVGGKALRPSQRVLLqaEQALL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  338 NAQRE--------STSLHDLNEKLEQELRHKEAQLKLHEEKI-GAIEEK-LELSEQKLAQHAKLQpdmeEQLKARMEALT 407
Cdd:PRK11281  205 NAQNDlqrkslegNTQLQDLLQKQRDYLTARIQRLEHQLQLLqEAINSKrLTLSEKTVQEAQSQD----EAARIQANPLV 280
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626414  408 KAQerhgsaedrirgLETNLdektnevvRLNQRL-----KMNE--EHNLRLSSTVDKLL-SESNerlqvhLKERMHAL 477
Cdd:PRK11281  281 AQE------------LEINL--------QLSQRLlkateKLNTltQQNLRVKNWLDRLTqSERN------IKEQISVL 332
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
324-491 4.85e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLH---------EEKIGAIEEKLELSEQKLAQHAKLQPD 394
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASSDD 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  395 ---MEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRL-----KMNEEHNLRLSSTVDKLLSESNER- 465
Cdd:COG4913   687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedLARLELRALLEERFAAALGDAVERe 766
                         170       180
                  ....*....|....*....|....*..
gi 442626414  466 LQVHLKERMHALDEK-NALTQELEKAR 491
Cdd:COG4913   767 LRENLEERIDALRARlNRAEEELERAM 793
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
64-537 5.02e-05

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: 47.66  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    64 RDVEKERDSLQRQINANLPQEF----ATLTKELTQARETLLERDEEIGELKAERN--NTRLLLEHLECLVSRHERSLRmT 137
Cdd:TIGR00618  196 AELLTLRSQLLTLCTPCMPDTYherkQVLEKELKHLREALQQTQQSHAYLTQKREaqEEQLKKQQLLKQLRARIEELR-A 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   138 VVKRQAAAQSGVSSEVEVLKalksLFEHHKALDEKVRERLRLSieknnmmeEELSSAKEELAQYKAGVVPAGVGSGSGAG 217
Cdd:TIGR00618  275 QEAVLEETQERINRARKAAP----LAAHIKAVTQIEQQAQRIH--------TELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   218 SAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKIS--ELEENMS 295
Cdd:TIGR00618  343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrTSAFRDL 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   296 RVQKEHCKAQDQCAKLQRDLRENVAQKEDQEEritTLEKRYLNaqrestslhdlneKLEQELRHKEAQLKLHEEKIGAIE 375
Cdd:TIGR00618  423 QGQLAHAKKQQELQQRYAELCAAAITCTAQCE---KLEKIHLQ-------------ESAQSLKEREQQLQTKEQIHLQET 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   376 EKLELSEQKLAQHAKLQPDMEEQLKARMEALTKA------QERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNL 449
Cdd:TIGR00618  487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   450 RLSSTVDKLLSESNErlqvhLKERMhaldekNALTQELEKARKVAEELhhEKSEIMKELSKTRLEIENFKRQLLQQEIAY 529
Cdd:TIGR00618  567 EIQQSFSILTQCDNR-----SKEDI------PNLQNITVRLQDLTEKL--SEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
                          490
                   ....*....|
gi 442626414   530 --NIQQTEAL 537
Cdd:TIGR00618  634 lqQCSQELAL 643
mukB PRK04863
chromosome partition protein MukB;
272-548 6.35e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  272 ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDL-RENVAQKEDQEERITTLE---KRYLNAQRESTSLH 347
Cdd:PRK04863  838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLpRLNLLADETLADRVEEIReqlDEAEEAKRFVQQHG 917
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  348 DLNEKLEQELrhkeAQLKLHEEKIGAIEEKLELSEQKLaqhaklqpdmeEQLKARMEALTKAQER--HGSAEDRIRGLET 425
Cdd:PRK04863  918 NALAQLEPIV----SVLQSDPEQFEQLKQDYQQAQQTQ-----------RDAKQQAFALTEVVQRraHFSYEDAAEMLAK 982
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  426 NLDekTNEvvRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVH--LKERMHAL-DEKNALTQEL------------EKA 490
Cdd:PRK04863  983 NSD--LNE--KLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLasLKSSYDAKrQMLQELKQELqdlgvpadsgaeERA 1058
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414  491 RKVAEELHHE-------KSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVD 548
Cdd:PRK04863 1059 RARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLR 1123
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
22-162 7.75e-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: 44.89  E-value: 7.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    22 SQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINA--------NLPqEFATLTKELT 93
Cdd:pfam15619   49 GKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRleklsedkNLA-EREELQKKLE 127
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626414    94 QARETLLERDEEIGELkaERnntrllleHLECLVSRHERSLRMTVVKrQAAAQSGVSSEVEVLKALKSL 162
Cdd:pfam15619  128 QLEAKLEDKDEKIQDL--ER--------KLELENKSFRRQLAAEKKK-HKEAQEEVKILQEEIERLQQK 185
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
304-521 7.93e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  304 AQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQlklheEKIGAIEEKLElseq 383
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELE---- 678
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  384 klaqhaklqpdmeeQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESN 463
Cdd:COG4913   679 --------------RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414  464 ERLQVHLKERMHALDEKNAltqelekARKVAEELHHEKSEIMKELSKTRLEIEN----FKRQ 521
Cdd:COG4913   745 LELRALLEERFAAALGDAV-------ERELRENLEERIDALRARLNRAEEELERamraFNRE 799
COG5022 COG5022
Myosin heavy chain [General function prediction only];
266-581 9.93e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.99  E-value: 9.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaqdqcakLQRDLRENVaqkEDQEERITTLEKRYLNAQ----- 340
Cdd:COG5022   880 AERQLQELKIDVKSISSLKLVNLELESEIIELKKS----------LSSDLIENL---EFKTELIARLKKLLNNIDleegp 946
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  341 -------RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAI---EEKLELSEQKLAQHAKLQPDMEEQLKaRMEALTKAQ 410
Cdd:COG5022   947 sieyvklPELNKLHEVESKLKETSEEYEDLLKKSTILVREGnkaNSELKNFKKELAELSKQYGALQESTK-QLKELPVEV 1025
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  411 ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLsstvdKLLSESNERLQVHLKERMHALDEKNALTQELEKA 490
Cdd:COG5022  1026 AELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARY-----KALKLRRENSLLDDKQLYQLESTENLLKTINVKD 1100
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  491 RKVAEElHHEKSE-----IMKELSKTRL--EIENFKRQLLqqeiaYNIQQTEALTRSLSPssvvDPSGAFSRSNSHASFE 563
Cdd:COG5022  1101 LEVTNR-NLVKPAnvlqfIVAQMIKLNLlqEISKFLSQLV-----NTLEPVFQKLSVLQL----ELDGLFWEANLEALPS 1170
                         330
                  ....*....|....*...
gi 442626414  564 THSLRRQSKQRLSEENAL 581
Cdd:COG5022  1171 PPPFAALSEKRLYQSALY 1188
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
36-522 1.14e-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: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    36 VSMLDERDKLMD-SLREAQERLNETENKLRDVEKerdSLQRQINAN--LPQEFATLTKELTQAREtllERDEEIGELKAE 112
Cdd:pfam05483  270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDIKM---SLQRSMSTQkaLEEDLQIATKTICQLTE---EKEAQMEELNKA 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   113 RNNTRLLLEHLECLVSRHERSLRmtvvkrqaAAQSGVSSEVEVLKALKslfehhKALDEKVRERLRLSIEKNNMmEEELS 192
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLR--------TEQQRLEKNEDQLKIIT------MELQKKSSELEEMTKFKNNK-EVELE 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   193 SAKEELAQyKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANElNDYAAKTHELQTIIEKQ--- 269
Cdd:pfam05483  409 ELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE-EHYLKEVEDLKTELEKEklk 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   270 TSELSQWQRRVSDLNNKISELEENMSRVQKEHckaqdqcaklQRDLRENVAQKEDQEERITTLEKRYLNAQREstsLHDL 349
Cdd:pfam05483  487 NIELTAHCDKLLLENKELTQEASDMTLELKKH----------QEDIINCKKQEERMLKQIENLEEKEMNLRDE---LESV 553
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   350 NEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKAR------MEALTKAQERHGSAED----- 418
Cdd:pfam05483  554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknieeLHQENKALKKKGSAENkqlna 633
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   419 ---RIRGLETNLD---EKTNEVVRLNQR----LKMNEEHNL----RLSSTVD---KLLSESNERLQVHLKErMHALDEKN 481
Cdd:pfam05483  634 yeiKVNKLELELAsakQKFEEIIDNYQKeiedKKISEEKLLeeveKAKAIADeavKLQKEIDKRCQHKIAE-MVALMEKH 712
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 442626414   482 A---------LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQL 522
Cdd:pfam05483  713 KhqydkiieeRDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQL 762
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1115-1186 1.21e-04

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: 41.51  E-value: 1.21e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414   1115 VLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDanamgLALQIPTQNAQARQILDTEFNNLLQ 1186
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLKE 67
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
945-1003 1.27e-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: 41.55  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414  945 WNGPTIVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 1003
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
248-489 1.63e-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: 46.19  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   248 EANEL-NDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRE---NVAQKE 323
Cdd:TIGR00606  692 ELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlknDIEEQE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHE------------EKIGAIEEKLELSEQKLAQHAKL 391
Cdd:TIGR00606  772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrtvqqvnQEKQEKQHELDTVVSKIELNRKL 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   392 QPDMEEQ---LKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQV 468
Cdd:TIGR00606  852 IQDQQEQiqhLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
                          250       260
                   ....*....|....*....|.
gi 442626414   469 HLKERMHALDEKNALTQELEK 489
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEKVKN 952
PRK12704 PRK12704
phosphodiesterase; Provisional
320-507 1.67e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  320 AQKEDQEERittlEKRYLNAQREstsLHDLNEKLEQELRHKEAQLKLHEEKIgaieeklelsEQKlaqhaklqpdmEEQL 399
Cdd:PRK12704   47 AKKEAEAIK----KEALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRL----------LQK-----------EENL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  400 KARMEALTKAQERhgsaedrirgletnLDEKTNEVVRLNQRLKMNEEhnlrlssTVDKLLSESNERLqvhlkERMHALDE 479
Cdd:PRK12704   99 DRKLELLEKREEE--------------LEKKEKELEQKQQELEKKEE-------ELEELIEEQLQEL-----ERISGLTA 152
                         170       180
                  ....*....|....*....|....*...
gi 442626414  480 KNALTQELEKARkvaEELHHEKSEIMKE 507
Cdd:PRK12704  153 EEAKEILLEKVE---EEARHEAAVLIKE 177
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-593 1.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   38 MLDERDkLMDSLREAQE---RLNETENKLRDVEKERDSLQrQINAnLPQEFATLTKELTQARE-----TLLERDEEIGEL 109
Cdd:COG4913   217 MLEEPD-TFEAADALVEhfdDLERAHEALEDAREQIELLE-PIRE-LAERYAAARERLAELEYlraalRLWFAQRRLELL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  110 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHH-KALDEKVRERLRLSiEKNNMME 188
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLeRELEERERRRARLE-ALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  189 EELSSAKEELAQYKAGVvpagvgsgsgagsaattaggggaenglkekmagvggsggvngeANELNDYAAKTHELQTIIEK 268
Cdd:COG4913   373 LPLPASAEEFAALRAEA-------------------------------------------AALLEALEEELEALEEALAE 409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  269 QTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQ-CAKL---QRDLR---ENVAQKEDQEERITTLEkRYLNAQR 341
Cdd:COG4913   410 AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEALgldEAELPfvgELIEVRPEEERWRGAIE-RVLGGFA 488
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  342 esTSL----------------HDLNEKLE-QELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAK---------LQPDM 395
Cdd:COG4913   489 --LTLlvppehyaaalrwvnrLHLRGRLVyERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEaelgrrfdyVCVDS 566
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  396 EEQLKARMEALTKA------QERH---------------GSAEDRIRGLETNLDEKTNEVVRLNQRL-KMNEEHN----- 448
Cdd:COG4913   567 PEELRRHPRAITRAgqvkgnGTRHekddrrrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLeALEAELDalqer 646
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  449 LRLSSTVDKLLSESNERLQVH-----LKERMHALDEKN----ALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFK 519
Cdd:COG4913   647 REALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626414  520 RQllqqeiaynIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHslRRQSKQRLSEENALVRSMAEQEWEKL 593
Cdd:COG4913   727 EE---------LDELQDRLEAAEDLARLELRALLEERFAAALGDAV--ERELRENLEERIDALRARLNRAEEEL 789
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-437 1.83e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  256 AAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEE---------NMSRVQKEHCKAQDQCAKLQ---RDLRENVAQKE 323
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEaelERLDASSDDLA 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  324 DQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEklelsEQKLAQHAKLQPDMEEQLKARM 403
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-----LARLELRALLEERFAAALGDAV 763
                         170       180       190
                  ....*....|....*....|....*....|....
gi 442626414  404 EALTKAQerhgsAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG4913   764 ERELREN-----LEERIDALRARLNRAEEELERA 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
41-203 2.06e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnlpqefatLTKELTQARETLLERDEEIGEL-----KAERNN 115
Cdd:COG4942    49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------LEKEIAELRAELEAQKEELAELlralyRLGRQP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  116 TRLLLEHLEcLVSRHERSLRM--TVVKRQAAAQSGVSSEVEVLKALKSLFEHHKA-----LDEKVRERLRLSIEKNNmME 188
Cdd:COG4942   121 PLALLLSPE-DFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAelealLAELEEERAALEALKAE-RQ 198
                         170
                  ....*....|....*
gi 442626414  189 EELSSAKEELAQYKA 203
Cdd:COG4942   199 KLLARLEKELAELAA 213
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
249-410 2.82e-04

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 44.28  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  249 ANELNDYAAKThelQTIIEKQTSELSQWQRRVSDLNNKiSELEENMSRVQ-------KEHCKAQDQCAKLQRDLRENVAQ 321
Cdd:cd22656    75 AGDIYNYAQNA---GGTIDSYYAEILELIDDLADATDD-EELEEAKKTIKallddllKEAKKYQDKAAKVVDKLTDFENQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  322 KEDQEERITTLEKRY------LNAQRESTSLHDLNEKLEQELRHKEAQLKlheEKIGAIEEKLELSEQKLAQHAKLQ--- 392
Cdd:cd22656   151 TEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLK---AKIDELKALIADDEAKLAAALRLIadl 227
                         170       180
                  ....*....|....*....|....*
gi 442626414  393 -------PDMEEQLKARMEALTKAQ 410
Cdd:cd22656   228 taadtdlDNLLALIGPAIPALEKLQ 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
267-677 4.43e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  267 EKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQR--DLRENVAQKEDQEERITTLEKRYLNAQREST 344
Cdd:COG4717    77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLE 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  345 SLHDLneklEQELRHKEAQLKLHEEKIGAIEEKLELS-EQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGL 423
Cdd:COG4717   157 ELREL----EEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  424 ETNLdektnEVVRLNQRLKMNEEHnLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSE 503
Cdd:COG4717   233 ENEL-----EAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  504 IMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRQSKQRL----SEEN 579
Cdd:COG4717   307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagveDEEE 386
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  580 ALVRSMAEQEWEKLQQAAHAQQQayELASAADCDDSDVLYAAATDMMSPSGHTDAQTLAM-----MLQEQLDAINNEIRL 654
Cdd:COG4717   387 LRAALEQAEEYQELKEELEELEE--QLEELLGELEELLEALDEEELEEELEELEEELEELeeeleELREELAELEAELEQ 464
                         410       420
                  ....*....|....*....|....*
gi 442626414  655 IQEEKQSTEARA--EELESRVGSLE 677
Cdd:COG4717   465 LEEDGELAELLQelEELKAELRELA 489
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
375-542 4.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  375 EEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEE-------- 446
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelgerara 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  447 --HNLRLSSTVDKLL-SESNERL--QVHLKERMHALDekNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQ 521
Cdd:COG3883    95 lyRSGGSVSYLDVLLgSESFSDFldRLSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
                         170       180
                  ....*....|....*....|.
gi 442626414  522 LLQQeiaynIQQTEALTRSLS 542
Cdd:COG3883   173 LEAQ-----QAEQEALLAQLS 188
COG5022 COG5022
Myosin heavy chain [General function prediction only];
307-589 5.47e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.30  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  307 QCAKLQRDLRENVAQKEdqEERITTLEKR-----YLNA----QRESTSLHDLNEKLEQELRHKEAQLKlheekigaieEK 377
Cdd:COG5022   783 LRRLVDYELKWRLFIKL--QPLLSLLGSRkeyrsYLACiiklQKTIKREKKLRETEEVEFSLKAEVLI----------QK 850
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  378 LELSEQKLAQHAKLQPD-MEEQLKARME-ALTKAQERHGSAEDRirgleTNLDEKTNEVVRLNQRLKMNEEHNLRLSStv 455
Cdd:COG5022   851 FGRSLKAKKRFSLLKKEtIYLQSAQRVElAERQLQELKIDVKSI-----SSLKLVNLELESEIIELKKSLSSDLIENL-- 923
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  456 dKLLSESNERLQVHLKER---------MHALDEKNALTQELEKARKVAEELHH--EKSEI-MKELSKTRLEIENFKRQLL 523
Cdd:COG5022   924 -EFKTELIARLKKLLNNIdleegpsieYVKLPELNKLHEVESKLKETSEEYEDllKKSTIlVREGNKANSELKNFKKELA 1002
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414  524 QQEIAYniqqtEALTRSLSPSSVVDPSGAFSRSNSHASFETHSlrrqSKQRLSEENALVRSMAEQE 589
Cdd:COG5022  1003 ELSKQY-----GALQESTKQLKELPVEVAELQSASKIISSEST----ELSILKPLQKLKGLLLLEN 1059
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
275-536 9.90e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.35  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   275 QWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLREN-------VAQKEDQEERITTLEKRYLN-AQRESTSL 346
Cdd:pfam07888   70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELseekdalLAQRAAHEARIRELEEDIKTlTQRVLERE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   347 HDLnEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAK-------LQPDMEEQLKARMEALTKAQERHGSAEDR 419
Cdd:pfam07888  150 TEL-ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqelrnSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   420 IRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTV---DKLLSESNE-RLQV------------HLKE-RMHALDEKNA 482
Cdd:pfam07888  229 EAENEALLEELRSLQERLNASERKVEGLGEELSSMAaqrDRTQAELHQaRLQAaqltlqladaslALREgRARWAQERET 308
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442626414   483 LTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:pfam07888  309 LQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
359-536 1.03e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  359 HKEAQLKLHEEKIGAIEEKLELSEQKLAQ-HAKLQPDMEEQLKARmEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRL 437
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQ-AELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  438 NQRLKMNEEHNLRLS---------------STVDKLLSESNERLQVHLKERmhalDEKNALTQELEKARKVAEELHHEKS 502
Cdd:COG3883    92 ARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADK----AELEAKKAELEAKLAELEALKAELE 167
                         170       180       190
                  ....*....|....*....|....*....|....
gi 442626414  503 EIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEA 536
Cdd:COG3883   168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
355-475 1.12e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  355 QELRHKEAQLKlhEEKIGAIEEKLELSEQKLAqhaKLQpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEV 434
Cdd:COG0542   414 DELERRLEQLE--IEKEALKKEQDEASFERLA---ELR-DELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626414  435 VRLNQRLKMNEE----HNLRLSSTVD-----------------KLLSESNERLQvHLKERMH 475
Cdd:COG0542   488 PELEKELAELEEelaeLAPLLREEVTeediaevvsrwtgipvgKLLEGEREKLL-NLEEELH 548
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
378-543 1.19e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  378 LELSE--QKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEhnlRLSST- 454
Cdd:COG1579    10 LDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---QLGNVr 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  455 ----VDKLLSE--SNERLQVHLKERMHALDEknaltqELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQlLQQEIA 528
Cdd:COG1579    87 nnkeYEALQKEieSLKRRISDLEDEILELME------RIEELEEELAELEAELAELEAELEEKKAELDEELAE-LEAELE 159
                         170
                  ....*....|....*
gi 442626414  529 YNIQQTEALTRSLSP 543
Cdd:COG1579   160 ELEAEREELAAKIPP 174
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
53-423 1.21e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    53 QERLNETENKLRDVEKERDSLQRQINANLPQeFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLV---SR 129
Cdd:TIGR00618  527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTeklSE 605
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   130 HERSLRmtvvkrqaaaqsgvssevEVLKALKSLFEHHKALdekvrerLRLSIEKNNMmEEELSSAKEELAQYKAGVVPAG 209
Cdd:TIGR00618  606 AEDMLA------------------CEQHALLRKLQPEQDL-------QDVRLHLQQC-SQELALKLTALHALQLTLTQER 659
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   210 VGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNdyaAKTHELQTIIEKQTSELSQWQR----RVSDLNN 285
Cdd:TIGR00618  660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ---TLLRELETHIEEYDREFNEIENasssLGSDLAA 736
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   286 KISELEENMS---RVQKEHCKAQDQcAKLQRDLRENVAQKEDQEER--ITTLEKRYLNAQRESTSLHDLNEKLEQELRHK 360
Cdd:TIGR00618  737 REDALNQSLKelmHQARTVLKARTE-AHFNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414   361 EAQLKLHEEKIGAIEE----KLELSEQKLAQHAKLQPDMEEQLKaRMEALTKAQERHGSAEDRIRGL 423
Cdd:TIGR00618  816 EDILNLQCETLVQEEEqflsRLEEKSATLGEITHQLLKYEECSK-QLAQLTQEQAKIIQLSDKLNGI 881
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
248-520 1.25e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   248 EANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRV---------------QKEHCKAQDQCAKLQ 312
Cdd:TIGR00606  246 ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhQRTVREKERELVDCQ 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   313 RDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGA---------IEEKLELSEQ 383
Cdd:TIGR00606  326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqiknfHTLVIERQED 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   384 KLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNE---VVRLNQRLKMNEEHNLRLSSTVDKLLS 460
Cdd:TIGR00606  406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRILELDQELRKAER 485
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414   461 E-----SNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKR 520
Cdd:TIGR00606  486 ElskaeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
248-526 1.34e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  248 EANELNDYAAKTHELQTIIEKQTSELSQwQRRvsDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:COG1340    16 KIEELREEIEELKEKRDELNEELKELAE-KRD--ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  328 RITTLEKRYLNAQRESTSLHDLNEKLEQ-ELRHKEAQLKLHEE-----KIGAIEEKLELSEQKLAQHAKLQpDMEEQLKA 401
Cdd:COG1340    93 ELDELRKELAELNKAGGSIDKLRKEIERlEWRQQTEVLSPEEEkelveKIKELEKELEKAKKALEKNEKLK-ELRAELKE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  402 RMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKlLSESNERLQVHLKERMHALDEKN 481
Cdd:COG1340   172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE-LHEEIIELQKELRELRKELKKLR 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 442626414  482 ALTQELEKaRKVAEELHHEKSEIMKELSKT-RLEIENFKrqLLQQE 526
Cdd:COG1340   251 KKQRALKR-EKEKEELEEKAEEIFEKLKKGeKLTTEELK--LLQKS 293
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
86-365 1.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   86 ATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVE----VLKALKS 161
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEE 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  162 LFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQykagvvpagvgsgsgagsaattaggggaenglkekmAGVGG 241
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE------------------------------------LQDRL 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  242 SGGVNGEANELNDYAAKTHElQTIIEKQTSELSQW-QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAklqRDLRENVA 320
Cdd:COG4913   737 EAAEDLARLELRALLEERFA-AALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLE 812
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442626414  321 QKEDQEERITTLE-----------KRYLNAQrESTSLHDLNEKLEQELRHKEAQLK 365
Cdd:COG4913   813 SLPEYLALLDRLEedglpeyeerfKELLNEN-SIEFVADLLSKLRRAIREIKERID 867
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
261-522 2.03e-03

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: 42.50  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   261 ELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAq 340
Cdd:pfam10174  356 EKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNT- 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   341 reSTSLHDLNEKLEQELRHKEAqlkLHEEKIGAIEEKLELSEQ--KLAQHAK-----LQPDMEEQLKARMEALTKAQERH 413
Cdd:pfam10174  435 --DTALTTLEEALSEKERIIER---LKEQREREDRERLEELESlkKENKDLKekvsaLQPELTEKESSLIDLKEHASSLA 509
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   414 GSA---EDRIRGLETNLDEKTNEVVRLNQRLK----------MNEEHNLRLS-----------------STVDKLL---- 459
Cdd:pfam10174  510 SSGlkkDSKLKSLEIAVEQKKEECSKLENQLKkahnaeeavrTNPEINDRIRlleqevarykeesgkaqAEVERLLgilr 589
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   460 -------------SESNERLQVHLKE--------RMHALDEKNALTQELEKARKVAEEL-----HHEKSEIMKELSKTRL 513
Cdd:pfam10174  590 evenekndkdkkiAELESLTLRQMKEqnkkvaniKHGQQEMKKKGAQLLEEARRREDNLadnsqQLQLEELMGALEKTRQ 669

                   ....*....
gi 442626414   514 EIENFKRQL 522
Cdd:pfam10174  670 ELDATKARL 678
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
32-179 2.20e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   32 EQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQIN---------------ANLPQEFATLTKELTQAR 96
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellqspviQQLRAQLAELEAELAELS 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   97 ETLLERDEEIGELKAERNNTRLLLehleclvsrhERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRER 176
Cdd:COG3206   284 ARYTPNHPDVIALRAQIAALRAQL----------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353

                  ...
gi 442626414  177 LRL 179
Cdd:COG3206   354 RRL 356
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-183 2.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   49 LREAQERLNETENKLRDVEKERDSLQRqinanLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVS 128
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  129 RHERSLRMTVV-----KRQAAAQSGVSSEVEvlkalKSLFEHHKALDEKvRERLRLSIEK 183
Cdd:COG4913   738 AAEDLARLELRalleeRFAAALGDAVERELR-----ENLEERIDALRAR-LNRAEEELER 791
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
280-513 2.50e-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: 41.76  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   280 VSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQ---------EERITTLEKRYLNAQRESTSLH--- 347
Cdd:pfam06160  181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEgyalehlnvDKEIQQLEEQLEENLALLENLElde 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   348 --DLNEKLEQELRHKEAQLklhEEKIGA---IEEKLELSEQKLaQHAKlqpDMEEQLKARMEALTKAQERHGSAEDRIRG 422
Cdd:pfam06160  261 aeEALEEIEERIDQLYDLL---EKEVDAkkyVEKNLPEIEDYL-EHAE---EQNKELKEELERVQQSYTLNENELERVRG 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   423 LETNLDEKTNEVVRLNQRLkmnEEHNLRLSSTVDKLLsESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKS 502
Cdd:pfam06160  334 LEKQLEELEKRYDEIVERL---EEKEVAYSELQEELE-EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
                          250
                   ....*....|.
gi 442626414   503 EIMKELSKTRL 513
Cdd:pfam06160  410 EIKRLVEKSNL 420
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
252-519 2.75e-03

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 42.03  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  252 LNDYAAKTHELQTIIEKQTS----ELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEE 327
Cdd:COG5192   418 IAEETSREDELSFDDSDVSTsdenEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKR 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  328 RITTLEKRYLnaqrESTSLHDLNEKLEQE-LRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:COG5192   498 GRNIQKIFYD----ESLSPEECIEEYKGEsAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELKKKWSSL 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  407 TKAQERH--GSAEDRIRGLE-----------------TNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDK-LLSESNERL 466
Cdd:COG5192   574 AQLKSRFqkDATLDSIEGEEeliqddekgnfedledeENSSDNEMEESRGSSVTAENEESADEVDYETEReENARKKEEL 653
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442626414  467 QVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFK 519
Cdd:COG5192   654 RGNFELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYR 706
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
251-489 2.99e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   251 ELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERIT 330
Cdd:pfam05557   28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   331 TLEKRYLNAQREStslhdlnEKLEQELRHKEAQLKlheekigAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQ 410
Cdd:pfam05557  108 CLKNELSELRRQI-------QRAELELQSTNSELE-------ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   411 --ERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDK--LLSESNERLQVHLKERMHALDEKNALTQE 486
Cdd:pfam05557  174 elEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENklLLKEEVEDLKRKLEREEKYREEAATLELE 253

                   ...
gi 442626414   487 LEK 489
Cdd:pfam05557  254 KEK 256
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
945-1008 3.00e-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: 37.25  E-value: 3.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626414   945 WNGPTIVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 1008
Cdd:pfam00536    3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
47-203 3.09e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   47 DSLREAQERLNETENKLRDVEKERDSLQRQINA-------------NLPQEFATLTKELTQARETLLERDEEIGELKAER 113
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEElneeynelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  114 NNTRLLLEHLECLVSrhERSL-----RMTVVKRQAAAQsgvSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMME 188
Cdd:COG3883    96 YRSGGSVSYLDVLLG--SESFsdfldRLSALSKIADAD---ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
                         170
                  ....*....|....*
gi 442626414  189 EELSSAKEELAQYKA 203
Cdd:COG3883   171 AELEAQQAEQEALLA 185
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
154-342 3.17e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  154 EVLKALKSLFEHHKALD--EKVRERLRLSIEKnnmMEEELSSAKEELAQYKAGVvpagvgsgsgagsAATTAGGGGAENG 231
Cdd:COG1579     4 EDLRALLDLQELDSELDrlEHRLKELPAELAE---LEDELAALEARLEAAKTEL-------------EDLEKEIKRLELE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  232 LKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIiekqtselsqwQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKL 311
Cdd:COG1579    68 IEEVEARIKKYEEQLGNVRNNKEYEALQKEIESL-----------KRRISDLEDEILELMERIEELEEELAELEAELAEL 136
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442626414  312 QRDLRENVAQKEDQEERITTLEKRyLNAQRE 342
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEE-LEAERE 166
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
37-376 3.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   37 SMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  117 RLLLEHLECLVSRHERSlRMTVVKRQAAAQSGVSSEVEVLKALKSlfehhkALDEKVRERLRLSIEKNNMMEEELSSAKE 196
Cdd:COG4372   114 QEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEE------QLESLQEELAALEQELQALSEAEAEQALD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  197 ELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQW 276
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  277 QRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQE 356
Cdd:COG4372   267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
                         330       340
                  ....*....|....*....|
gi 442626414  357 LRHKEAQLKLHEEKIGAIEE 376
Cdd:COG4372   347 LVGLLDNDVLELLSKGAEAG 366
PTZ00121 PTZ00121
MAEBL; Provisional
41-588 4.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   41 ERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQinanlpQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLL 120
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  121 EHLEcLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDE--------KVRERLRLSIEKNNMMEEELS 192
Cdd:PTZ00121 1425 KKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeaKKADEAKKKAEEAKKKADEAK 1503
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  193 SAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELN--DYAAKTHELQTIIEKQT 270
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKkaEEAKKAEEDKNMALRKA 1583
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  271 SELSQWQRRVSDLNNKISELEENM----------SRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQ 340
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMkaeeakkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  341 RESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQE-RHGSAEDR 419
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDK 1743
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  420 IRGLETNLDEKTNEVVrlnQRLKMNEEhnlrlsstvdKLLSESNERLQVHLKERMHALDEKNALTQElekaRKVAEELhh 499
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKI---AHLKKEEE----------KKAEEIRKEKEAVIEEELDEEDEKRRMEVD----KKIKDIF-- 1804
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  500 EKSEIMKELSKTRLEIENFKRQLLQQEI-----AYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRqskqr 574
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIkevadSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKED----- 1879
                         570
                  ....*....|....
gi 442626414  575 lSEENALVRSMAEQ 588
Cdd:PTZ00121 1880 -DEEEIEEADEIEK 1892
mukB PRK04863
chromosome partition protein MukB;
266-504 4.30e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  266 IEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEhckaQDQCAKLQRDLRENVAQKEDQEERITTL----EKR----YL 337
Cdd:PRK04863  899 IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRahfsYE 974
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  338 NAQRESTSLHDLNEKLEQELRHKEAQlklheekigaieekleLSEQKlaqhaklqpdmeEQLKARMEALTKAQERHGSAE 417
Cdd:PRK04863  975 DAAEMLAKNSDLNEKLRQRLEQAEQE----------------RTRAR------------EQLRQAQAQLAQYNQVLASLK 1026
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  418 DRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRL-SSTVDKLLSESNERLQVHLKERMHALDEKNALTQeleKARKVAEE 496
Cdd:PRK04863 1027 SSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTK---KLRKLERD 1103

                  ....*...
gi 442626414  497 LHHEKSEI 504
Cdd:PRK04863 1104 YHEMREQV 1111
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
250-429 5.45e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 40.01  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRvqkehckAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:pfam00261    8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER-------TEERLAEALEKLEEAEKAADESERGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   330 TTLEKRylnAQRESTSLHDLNEKLEQ-ELRHKEAQLKLHE--EKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEAL 406
Cdd:pfam00261   81 KVLENR---ALKDEEKMEILEAQLKEaKEIAEEADRKYEEvaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNL 157
                          170       180       190
                   ....*....|....*....|....*....|
gi 442626414   407 -------TKAQERHGSAEDRIRGLETNLDE 429
Cdd:pfam00261  158 ksleaseEKASEREDKYEEQIRFLTEKLKE 187
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-203 5.60e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   40 DERDKLMDS---LREAQERLNETENKLRDVEKERDSLQRQINAnLPQEFATLTKELTQARETLLERDEEIGELKAERNNT 116
Cdd:COG4913   675 AELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  117 RLLLEHLECLVSRHERSLRmtvvKRQAAAQSGVSSEVEvlkALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSS-AK 195
Cdd:COG4913   754 RFAAALGDAVERELRENLE----ERIDALRARLNRAEE---ELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEE 826

                  ....*...
gi 442626414  196 EELAQYKA 203
Cdd:COG4913   827 DGLPEYEE 834
RNase_Y_N pfam12072
RNase Y N-terminal region;
396-507 5.91e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   396 EEQLKARMEALTKAQERHG---SAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQvhlkE 472
Cdd:pfam12072   60 EEIHKLRAEAERELKERRNelqRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIE----E 135
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 442626414   473 RMHALDEKNALTQELEKAR---KVAEELHHEKSEIMKE 507
Cdd:pfam12072  136 QRQELERISGLTSEEAKEIlldEVEEELRHEAAVMIKE 173
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
250-472 6.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  250 NELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERI 329
Cdd:COG4372    80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  330 TTLEKRY--LNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALT 407
Cdd:COG4372   160 ESLQEELaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626414  408 KAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKE 472
Cdd:COG4372   240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
345-539 6.99e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  345 SLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQhaklqpdMEEQLKARMEALTKAQERHGSAEDRIRGLE 424
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ-------AREELEQLEEELEQARSELEQLEEELEELN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  425 TNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSEsNERLQvhlkermhalDEKNALTQELEKARKVAEELHHEKSEI 504
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-RQDLE----------QQRKQLEAQIAELQSEIAEREEELKEL 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 442626414  505 MKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTR 539
Cdd:COG4372   156 EEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-193 7.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   39 LDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINanlPQEFATLTKELTQARETLLERDEEIGELKAERNNTRL 118
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS---EEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414  119 LLEHLeclvsrherslrmtvvKRQAAAQSGVSSEVEVL-KALKSLfehhKALDEKVReRLRLSIEKNNMME-EELSS 193
Cdd:PRK03918  695 TLEKL----------------KEELEEREKAKKELEKLeKALERV----EELREKVK-KYKALLKERALSKvGEIAS 750
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
291-526 7.69e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   291 EENMSRVQKEHCKAQDQCAKLQRDLREnVAQKEDQ--EERITTLEKR------YLNAQRESTSLHDLNEKLEQELRHKEA 362
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKE-LEKKHQQlcEEKNALQEQLqaetelCAEAEEMRARLAARKQELEEILHELES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   363 QLKLHEEKigaiEEKLELSEQKLAQHAKlqpDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLK 442
Cdd:pfam01576   83 RLEEEEER----SQQLQNEKKKMQQHIQ---DLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   443 MNEEHNLRLSSTV------DKLLSESNERLQVHLKERMHALDEKNALTQELEKARKvaeELHHEKSEIMKELSKTRLEIE 516
Cdd:pfam01576  156 LLEERISEFTSNLaeeeekAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR---KLEGESTDLQEQIAELQAQIA 232
                          250
                   ....*....|
gi 442626414   517 NFKRQLLQQE 526
Cdd:pfam01576  233 ELRAQLAKKE 242
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
270-539 7.77e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  270 TSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQ-KEDQEERITTLEK-RYLNAQREST--S 345
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaQELREKRDELNEKvKELKEERDELneK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  346 LHDLNEKLEqELRHKEAQLKLHEEKIGAIEEKLELSEQKLaQHAKLQPDMEEQLKARMEALTKAQErhgsAEDRIRGLET 425
Cdd:COG1340    87 LNELREELD-ELRKELAELNKAGGSIDKLRKEIERLEWRQ-QTEVLSPEEEKELVEKIKELEKELE----KAKKALEKNE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  426 NLDEKTNEVVRLnqRLKMNEEHnlrlsstvdKLLSESNERLQVHLKERmhaldekNALTQELEKARKVAEELHHEKSEIM 505
Cdd:COG1340   161 KLKELRAELKEL--RKEAEEIH---------KKIKELAEEAQELHEEM-------IELYKEADELRKEADELHKEIVEAQ 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 442626414  506 KELSKTRLEIENFKRQL--LQQEIAYNIQQTEALTR 539
Cdd:COG1340   223 EKADELHEEIIELQKELreLRKELKKLRKKQRALKR 258
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
275-409 8.16e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  275 QWQRRVSDLNNKISELEENMSRVQKEHCKAQDQcAKLQRDLRENVAQKEDQ--EERITTLEKRYLNAQRESTSLHDLNEK 352
Cdd:PRK09510   84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEAEAKRAAAAAKK 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442626414  353 LEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKA 409
Cdd:PRK09510  163 AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
46 PHA02562
endonuclease subunit; Provisional
353-522 8.31e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  353 LEQELRHKEAQLKLHEEKIGAIEEK----LELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLD 428
Cdd:PHA02562  186 LDMKIDHIQQQIKTYNKNIEEQRKKngenIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414  429 EKTNEVVRLNQRLKMNEEHNLrlSSTVDKLLSESNERLQvHLKERMHALDEKnalTQELEKARKVAEELHHEKSEIMKEL 508
Cdd:PHA02562  266 KIKSKIEQFQKVIKMYEKGGV--CPTCTQQISEGPDRIT-KIKDKLKELQHS---LEKLDTAIDELEEIMDEFNEQSKKL 339
                         170
                  ....*....|....
gi 442626414  509 SKTRLEIENFKRQL 522
Cdd:PHA02562  340 LELKNKISTNKQSL 353
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
45-527 8.32e-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: 40.49  E-value: 8.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414    45 LMDSLREAQERLNETENKLRDvEKERDSLQRQINANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLE 124
Cdd:pfam05557   53 LQKRIRLLEKREAEAEEALRE-QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTN 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   125 CLVSRHERSLRMTVVKRQAAAQSGVSSEvevlKALKSLFEHhkalDEKVRErLRLSIEKNNMMEEELSSAKEELAQykag 204
Cdd:pfam05557  132 SELEELQERLDLLKAKASEAEQLRQNLE----KQQSSLAEA----EQRIKE-LEFEIQSQEQDSEIVKNSKSELAR---- 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   205 vVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEanelnDYAAKTHELQTIIEKQTSELSQWQRrvsdln 284
Cdd:pfam05557  199 -IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVK------ 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   285 nkiseleenmsrvqkehcKAQDQCAKLQRdlrenvaqKEDQEERITTLEKRYLNAQRESTSlhdlnekLEQELRHKEAQL 364
Cdd:pfam05557  267 ------------------LAQDTGLNLRS--------PEDLSRRIEQLQQREIVLKEENSS-------LTSSARQLEKAR 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   365 KLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLkarmeaLTKAQERhgsaeDRIRGLETNLDEK---TNEVVRLNQRL 441
Cdd:pfam05557  314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV------LLLTKER-----DGYRAILESYDKEltmSNYSPQLLERI 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626414   442 KMNEEhnlrLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKvaEELHHEKSEIMKELSKTRLEIEN--FK 519
Cdd:pfam05557  383 EEAED----MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ--QESLADPSYSKEEVDSLRRKLETleLE 456

                   ....*...
gi 442626414   520 RQLLQQEI 527
Cdd:pfam05557  457 RQRLREQK 464
 
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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