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Conserved domains on  [gi|1720361586|ref|XP_030100997|]
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liprin-alpha-2 isoform X1 [Mus musculus]

Protein Classification

liprin-alpha( domain architecture ID 13527058)

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_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
1111-1182 3.26e-44

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: 154.01  E-value: 3.26e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1111 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1182
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
902-972 4.59e-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: 153.87  E-value: 4.59e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361586  902 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 972
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
1026-1091 1.20e-43

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


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586 1026 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1091
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-533 1.30e-15

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.41  E-value: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLTGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  200 ERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgsTESEHLEGMEAGQK--VHEKRLSNGSIDS-------------- 263
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGILGVlselisvdegyeaa 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 -------------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI 326
Cdd:TIGR02168  539 ieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  327 RecYL-------------QAMAQKEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQ 388
Cdd:TIGR02168  619 S--YLlggvlvvddldnaLELAKKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAE 695
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 464
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  465 HNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 533
Cdd:TIGR02168  776 ELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
 
Name Accession Description Interval E-value
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 ...
1111-1182 3.26e-44

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: 154.01  E-value: 3.26e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1111 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1182
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
902-972 4.59e-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: 153.87  E-value: 4.59e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361586  902 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 972
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
1026-1091 1.20e-43

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586 1026 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1091
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-533 1.30e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.41  E-value: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLTGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  200 ERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgsTESEHLEGMEAGQK--VHEKRLSNGSIDS-------------- 263
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGILGVlselisvdegyeaa 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 -------------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI 326
Cdd:TIGR02168  539 ieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  327 RecYL-------------QAMAQKEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQ 388
Cdd:TIGR02168  619 S--YLlggvlvvddldnaLELAKKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAE 695
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 464
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  465 HNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 533
Cdd:TIGR02168  776 ELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
189-545 2.94e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 2.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLrvslERVSALEEELAA-----ANQEIVALREQNVhiqrkmvssegSTESEHLEGMEAGQKVHEKRLsngsiDS 263
Cdd:COG1196    182 EATEENL----ERLEDILGELERqleplERQAEKAERYREL-----------KEELKELEAELLLLKLRELEA-----EL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqrdirecyLQAMAQKEDMEER 343
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------------YELLAELARLEQD 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAA 423
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEE 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  424 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQ 503
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEE 456
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 545
Cdd:COG1196    457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1025-1089 6.28e-14

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: 67.68  E-value: 6.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586 1025 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-543 4.31e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.92  E-value: 4.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI 261
Cdd:PRK02224   264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  262 DSTDDTSQIVELQEllekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDME 341
Cdd:PRK02224   336 AAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELE 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQ 419
Cdd:PRK02224   391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSP 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  420 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-E 496
Cdd:PRK02224   466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrE 544
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1720361586  497 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 543
Cdd:PRK02224   545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-537 4.27e-10

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: 64.37  E-value: 4.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDR------------------DSLQRQLNS--ALPQDIESLTGGLTGSKG 97
Cdd:pfam15921  122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHELeaakclkedmledsntqiEQLRKMMLSheGVLQEIRSILVDFEEASG 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   98 ADPPE-------------------FAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHERSL- 152
Cdd:pfam15921  202 KKIYEhdsmstmhfrslgsaiskiLRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEIt 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  153 ----RMTVVKRQAQSpsgVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEI 216
Cdd:pfam15921  282 glteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  217 VALReqnvhIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLS-----NGSIDSTDDTSQIV--ELQELLEKQNYEMAQMKE 289
Cdd:pfam15921  359 TEAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEVQRLEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  290 RLTALSSRV-GEVEQEAETARKdliKTEEMntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKL 368
Cdd:pfam15921  434 LLKAMKSECqGQMERQMAAIQG---KNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  369 EnelaNKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEERH 431
Cdd:pfam15921  506 Q----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQH 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  432 GNIEERMR----HLEGQLEEKNQELQRAR----QREKMNEEHNKRLSD---TVDRLLTESNERL-----------QLhLK 489
Cdd:pfam15921  582 GRTAGAMQvekaQLEKEINDRRLELQEFKilkdKKDAKIRELEARVSDlelEKVKLVNAGSERLravkdikqerdQL-LN 660
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  490 ERMAALEEKNVLIQESE----NFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:pfam15921  661 EVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
902-968 5.11e-09

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: 53.84  E-value: 5.11e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586   902 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 968
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1034-1089 1.12e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.12e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  1034 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1112-1183 6.63e-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: 47.68  E-value: 6.63e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  1112 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1183
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
904-968 1.20e-04

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: 41.10  E-value: 1.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  904 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 968
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1112-1182 1.41e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.41e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586 1112 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1182
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
366-540 1.49e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  366 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 433
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  434 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 503
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720361586  504 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 540
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
 
Name Accession Description Interval E-value
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 ...
1111-1182 3.26e-44

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: 154.01  E-value: 3.26e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1111 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1182
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
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 ...
902-972 4.59e-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: 153.87  E-value: 4.59e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361586  902 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 972
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
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 ...
1026-1091 1.20e-43

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 152.24  E-value: 1.20e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586 1026 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1091
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
1030-1089 2.32e-31

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: 117.25  E-value: 2.32e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586 1030 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
909-967 3.09e-27

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: 105.39  E-value: 3.09e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  909 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 967
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
1119-1180 6.91e-25

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: 98.77  E-value: 6.91e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1119 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1180
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 ...
1111-1182 1.43e-18

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: 80.95  E-value: 1.43e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1111 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1182
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
903-967 4.98e-17

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: 76.72  E-value: 4.98e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  903 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 967
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
1025-1089 1.70e-16

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: 74.75  E-value: 1.70e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586 1025 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1089
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 ...
1025-1089 1.94e-16

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: 74.65  E-value: 1.94e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586 1025 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-533 1.30e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.41  E-value: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLTGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  200 ERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgsTESEHLEGMEAGQK--VHEKRLSNGSIDS-------------- 263
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGILGVlselisvdegyeaa 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 -------------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI 326
Cdd:TIGR02168  539 ieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  327 RecYL-------------QAMAQKEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQ 388
Cdd:TIGR02168  619 S--YLlggvlvvddldnaLELAKKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAE 695
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 464
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  465 HNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 533
Cdd:TIGR02168  776 ELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
1111-1182 2.15e-15

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 72.10  E-value: 2.15e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1111 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1182
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
276-539 7.83e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.10  E-value: 7.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  276 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 355
Cdd:TIGR02168  672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  356 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 431
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  432 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 505
Cdd:TIGR02168  817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720361586  506 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-485 1.89e-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: 78.56  E-value: 1.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  101 PEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 177
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  178 KSLFEHHKALDEK---VRERLRVSLERVSALEEELAAANQEivaLREQNVHIQRKmvssegstesehlegmEAGQKVHEK 254
Cdd:TIGR02168  771 EEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAE---LTLLNEEAANL----------------RERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  255 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 334
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-----------ALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDMEERITTLEKRYLSAQresTSIHDMNDKLEnelankeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEV 413
Cdd:TIGR02168  901 EELRELESKRSELRRELEELR---EKLAQLELRLE-----------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDD 966
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  414 EAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLl 477
Cdd:TIGR02168  967 EEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV- 1041

                   ....*...
gi 1720361586  478 tesNERLQ 485
Cdd:TIGR02168 1042 ---NENFQ 1046
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
189-545 2.94e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 2.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLrvslERVSALEEELAA-----ANQEIVALREQNVhiqrkmvssegSTESEHLEGMEAGQKVHEKRLsngsiDS 263
Cdd:COG1196    182 EATEENL----ERLEDILGELERqleplERQAEKAERYREL-----------KEELKELEAELLLLKLRELEA-----EL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqrdirecyLQAMAQKEDMEER 343
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------------YELLAELARLEQD 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAA 423
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEE 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  424 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQ 503
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEE 456
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 545
Cdd:COG1196    457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-487 3.06e-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: 78.17  E-value: 3.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  114 REQLLEKEEEISELKAERNNTRLLLEH-------LECLVSRHERSLRMtvVKRQAQspsgvssevevlKALKslfehHKA 186
Cdd:TIGR02168  157 RRAIFEEAAGISKYKERRKETERKLERtrenldrLEDILNELERQLKS--LERQAE------------KAER-----YKE 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  187 LDEKVRE-RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGS---TESEHLEgMEAGQKVHEKRLSNGSID 262
Cdd:TIGR02168  218 LKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE-LEEEIEELQKELYALANE 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  263 STDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQrDIRECYLQAMAQKEDMEE 342
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---KLEELKEELE-SLEAELEELEAELEELES 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  343 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELAQR 420
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEEL 452
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  421 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 487
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1025-1089 6.28e-14

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: 67.68  E-value: 6.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586 1025 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
114-537 6.60e-14

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 77.03  E-value: 6.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 193
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  194 RLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehLEGMEAgqKVHEKRLSNGSIDSTDDTSQIVEL 273
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEAR-------------------IEELEE--DLHKLEEALNDLEARLSHSRIPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  274 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdliktEEMNTKyQRDIRECylqaMAQKEDMEERITTLEKRYls 353
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDL----KEQIKSIEKEIENLNGKK-- 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  354 aqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGN 433
Cdd:TIGR02169  864 ------------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEA 928
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  434 IEERMRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESENFR 509
Cdd:TIGR02169  929 LEEELSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVL 985
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1720361586  510 KNLEESLHDKERLAEE---IEKLRSELDQMK 537
Cdd:TIGR02169  986 KRLDELKEKRAKLEEErkaILERIEEYEKKK 1016
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
182-497 2.32e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.97  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRER-LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRlsngs 260
Cdd:COG1196    213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  261 idstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqAMAQKEDM 340
Cdd:COG1196    288 -------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEA 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  341 EERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmRKAETLPEVEAELAQR 420
Cdd:COG1196    357 EAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEAL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  421 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 497
Cdd:COG1196    431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-543 4.31e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 73.92  E-value: 4.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI 261
Cdd:PRK02224   264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  262 DSTDDTSQIVELQEllekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDME 341
Cdd:PRK02224   336 AAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELE 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQ 419
Cdd:PRK02224   391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSP 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  420 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-E 496
Cdd:PRK02224   466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrE 544
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1720361586  497 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 543
Cdd:PRK02224   545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-516 6.47e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 6.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDSTDD 266
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqiSALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqrdirecylqamAQKEDMEERITT 346
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------------------AELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTK 426
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----------ALLNERASLEEALAL 891
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  427 AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE 506
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
                          330
                   ....*....|
gi 1720361586  507 NFRKNLEESL 516
Cdd:TIGR02168  972 RRLKRLENKI 981
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
902-966 1.39e-12

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: 63.79  E-value: 1.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  902 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 966
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
290-535 5.47e-12

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: 70.47  E-value: 5.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  290 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC---YLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMND 366
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQKELYALANE---ISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  367 KLENELANKEAILRQMEEKNRQLQE----RLELAEQKLQQTMRKAETLPEVEAELAQriaaLTKAEERHGNIEERMRHLE 442
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  443 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESENFRKNLEESLHDKE 520
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELE 457
                          250
                   ....*....|....*
gi 1720361586  521 RLAEEIEKLRSELDQ 535
Cdd:TIGR02168  458 RLEEALEELREELEE 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-536 3.56e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 3.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGgltgskgadppEFAALTKELNACREQLLE 119
Cdd:COG1196    274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEE-----------ELAELEEELEELEEELEE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTV------VKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRE 193
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVEL 273
Cdd:COG1196    422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  274 QELLEKQNYEMAQMKERLTALSSRVG-----EVEQEAETARKDLIKTEEMNTKYQRDIREC--YLQAMAQKEDMEERITT 346
Cdd:COG1196    502 DYEGFLEGVKAALLLAGLRGLAGAVAvligvEAAYEAALEAALAAALQNIVVEDDEVAAAAieYLKAAKAGRATFLPLDK 581
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQ-RESTSIHDMNDKLENELANKEAILR--QMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 423
Cdd:COG1196    582 IRARAALAAaLARGAIGAAVDLVASDLREADARYYvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  424 LTKAEERHGN-----IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK 498
Cdd:COG1196    662 LTGGSRRELLaalleAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1720361586  499 NVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 536
Cdd:COG1196    742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-535 1.03e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.24  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  115 EQLLEKEEEISELKAERNNTRLLLEhleclvsrherslrmtvvkrqaqspsGVSSEVEVLKALKSLFEHHKALDEKVRER 194
Cdd:PRK03918   200 KELEEVLREINEISSELPELREELE--------------------------KLEKEVKELEELKEEIEELEKELESLEGS 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  195 LRVSLERVSALEEELAAANQEIVALREqnvhiQRKMVSSEGSTESEHLEgMEAGQKVHEKRLSNGSIDSTDDTSQIVELQ 274
Cdd:PRK03918   254 KRKLEEKIRELEERIEELKKEIEELEE-----KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  275 EL---LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQR-------DIRECYLQAMAQKEDMEERI 344
Cdd:PRK03918   328 ERikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeKLEKELEELEKAKEEIEEEI 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  345 TTLEKRYLSAQRESTSIHDMNDKLEN--------------------------ELANKEAILRQMEEKNRQLQERLELAEQ 398
Cdd:PRK03918   408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRELEK 487
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  399 KLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsD 471
Cdd:PRK03918   488 VLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL-D 566
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  472 TVDRLLTESNERLQLHLKERMAALEEKnvlIQESENFRK---NLEESLHDKERLAEEIEKLRSELDQ 535
Cdd:PRK03918   567 ELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELEREEKELKKLEEELDK 630
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-539 1.22e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.24  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918   232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES-EHLEGMEAGQKVHEKRLSNGS 260
Cdd:PRK03918   306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  261 IDstddtsQIVELQELLEKQNYEMaqmKERLTALSSRVGEVEQEAETARKDLIKTE-----------EMNTKYQRDIREC 329
Cdd:PRK03918   386 PE------KLEKELEELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEE 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  330 YLqamAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAI--LRQMEEKNRQLQERLE-LAEQKLQQTMRK 406
Cdd:PRK03918   457 YT---AELKRIEKELKEIEEKERKLRKELR-------ELEKVLKKESELikLKELAEQLKELEEKLKkYNLEELEKKAEE 526
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  407 AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQ 485
Cdd:PRK03918   527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLE 606
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  486 LHLKERMAALEEKNVLIQESEnfrknLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:PRK03918   607 LKDAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLEELRKELEELEKK 655
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
169-464 1.61e-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: 65.86  E-value: 1.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  169 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMVSSEGSTESehlegMEA 247
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIAS-----LER 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  248 GQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIR 327
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRD 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  328 EcylqamaqKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqtmRKA 407
Cdd:TIGR02169  386 E--------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----------DKA 447
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  408 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 464
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-461 3.88e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.02  E-value: 3.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVSS 169
Cdd:COG4717     89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEEL 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  170 EVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEgmeagQ 249
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----E 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  250 KVHEKRLSN----------GSIDSTDDTSQIVE------------LQELLEKQNYEMAQMKERLTALSSRvgevEQEAET 307
Cdd:COG4717    244 RLKEARLLLliaaallallGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPAL----EELEEE 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  308 ARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnR 387
Cdd:COG4717    320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-Q 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  388 QLQERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQRE 459
Cdd:COG4717    399 ELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQEL 478

                   ..
gi 1720361586  460 KM 461
Cdd:COG4717    479 EE 480
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-537 4.27e-10

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: 64.37  E-value: 4.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDR------------------DSLQRQLNS--ALPQDIESLTGGLTGSKG 97
Cdd:pfam15921  122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHELeaakclkedmledsntqiEQLRKMMLSheGVLQEIRSILVDFEEASG 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   98 ADPPE-------------------FAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHERSL- 152
Cdd:pfam15921  202 KKIYEhdsmstmhfrslgsaiskiLRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEIt 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  153 ----RMTVVKRQAQSpsgVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEI 216
Cdd:pfam15921  282 glteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  217 VALReqnvhIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLS-----NGSIDSTDDTSQIV--ELQELLEKQNYEMAQMKE 289
Cdd:pfam15921  359 TEAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEVQRLEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  290 RLTALSSRV-GEVEQEAETARKdliKTEEMntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKL 368
Cdd:pfam15921  434 LLKAMKSECqGQMERQMAAIQG---KNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  369 EnelaNKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEERH 431
Cdd:pfam15921  506 Q----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQH 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  432 GNIEERMR----HLEGQLEEKNQELQRAR----QREKMNEEHNKRLSD---TVDRLLTESNERL-----------QLhLK 489
Cdd:pfam15921  582 GRTAGAMQvekaQLEKEINDRRLELQEFKilkdKKDAKIRELEARVSDlelEKVKLVNAGSERLravkdikqerdQL-LN 660
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  490 ERMAALEEKNVLIQESE----NFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:pfam15921  661 EVKTSRNELNSLSEDYEvlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-537 5.45e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.93  E-value: 5.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 192
Cdd:PRK03918   286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEagQKVHEKRLSNGSIDSTDDTSQIV 271
Cdd:PRK03918   364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 -------ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----RDIRECY-------LQ 332
Cdd:PRK03918   442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlKELEEKLkkynleeLE 521
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  333 AMAQK-EDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 404
Cdd:PRK03918   522 KKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  405 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 484
Cdd:PRK03918   602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  485 QLHLKERMAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:PRK03918   675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-544 6.74e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  104 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 180
Cdd:PRK03918   168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  181 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiqRKMVSSEGSTESEHLEgMEAGQKVHEKRLSNGS 260
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-----VKELKELKEKAEEYIK-LSEFYEEYLDELREIE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  261 IDSTDDTSQIVELQELLEKqnyemaqmkerLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdirecYLQAMAQKEDM 340
Cdd:PRK03918   314 KRLSRLEEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERL 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  341 EERIT-----TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAET 409
Cdd:PRK03918   378 KKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKEL 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  410 LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLK 489
Cdd:PRK03918   454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LK 531
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  490 ERMAALEEKnvliqesenfRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLI 544
Cdd:PRK03918   532 EKLIKLKGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-533 9.46e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 9.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918   315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMVSSEGSTESE 240
Cdd:PRK03918   395 ELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEE 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  241 HLEGMEAGQKVHEKRLSNGS--IDSTDDTSQIVELQELLEKQNYEMAQMKER-LTALSSRVGEVEQEAETARKDLIKTEE 317
Cdd:PRK03918   474 KERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEE 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  318 MNTKYQRDIREcylqamaqKEDMEERITTLEKRYLSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQ 388
Cdd:PRK03918   554 LKKKLAELEKK--------LDELEEELAELLKELEELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKK 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHN 466
Cdd:PRK03918   624 LEEELDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EEL 685
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  467 KRLSDTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESENFRKNLEeslhDKERLAEEIEKLRSEL 533
Cdd:PRK03918   686 EKRREEIKKTLEK--------LKEELEEREKA---KKELEKLEKALE----RVEELREKVKKYKALL 737
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
39-536 1.23e-09

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: 63.06  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLTGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRM-TVVKRQAQSPSGVSSEVEvlKALKSLFEHHKALDEK--VRE 193
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPgpLTR 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTE------SEHLEGMEAGQKVHEKRLSNGSIDSTDDT 267
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 SQIVELQELLEKQNYEMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTL 347
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQDLQDVRLH-------LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  348 EKRYLSAQRESTSIHDM----NDKLENELANKEAILRQMEE-------KNRQLQERLELAEQKLQQTMRKAET-LPEVEA 415
Cdd:TIGR00618  682 LQKMQSEKEQLTYWKEMlaqcQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTvLKARTE 761
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  416 ELAQRIAALTKAEERhgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL 495
Cdd:TIGR00618  762 AHFNNNEEVTAALQT----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1720361586  496 EEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 536
Cdd:TIGR00618  838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
PTZ00121 PTZ00121
MAEBL; Provisional
109-518 3.21e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  109 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 188
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVHEKRLSNgSIDSTDD 266
Cdd:PTZ00121  1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdlikTEEMNTKYQRdirECYLQAMAQKEDMEERITT 346
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-----IEEVMKLYEE---EKKMKAEEAKKAEEAKIKA 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAEL 417
Cdd:PTZ00121  1623 EELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEE 1700
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  418 AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAA 494
Cdd:PTZ00121  1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
                          410       420
                   ....*....|....*....|....
gi 1720361586  495 LEEKnvLIQESENFRKNLEESLHD 518
Cdd:PTZ00121  1781 IEEE--LDEEDEKRRMEVDKKIKD 1802
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
53-530 3.54e-09

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 61.60  E-value: 3.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   53 QESLSLAQQRLQDVIYDRDSLQRQLNSALPQDI--------ESLTGGLTGSKGADPPEFAALTKELNACREQLLEKEEEI 124
Cdd:TIGR00606  349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGfergpfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQA 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  125 SELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVSSEV-EVLKAL-KSLFEHHKALDEKVRERLrvsLERV 202
Cdd:TIGR00606  429 DEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIlELDQELrKAERELSKAEKNSLTETL---KKEV 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  203 SALEEELAAANQEIVALREQNVHIQRKmVSSEGSTESEHLEGMEAGQKVHE--KRLSNGSIDSTDDTSQIVELQELLEKQ 280
Cdd:TIGR00606  504 KSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKikSRHSDELTSLLGYFPNKKQLEDWLHSK 582
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  281 NYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqaMAQKEDMEERITTLEKRYLSAQRESTS 360
Cdd:TIGR00606  583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDLERLKEEIEKSSKQRAM 657
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  361 IH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA----QRIAALTKAEERHG 432
Cdd:TIGR00606  658 LAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQS 737
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  433 NIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQLHLKERMAALEEKNVLIQ 503
Cdd:TIGR00606  738 IIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQMELKDVERKIAQQAAKLQ 816
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1720361586  504 ESE------NFRKNLEESLHDKERLAEEIEKLR 530
Cdd:TIGR00606  817 GSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
335-543 4.39e-09

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: 61.24  E-value: 4.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET----L 410
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  411 PEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqrEKMNEEHnKRLSDTVDRLLTESNERLQL--HL 488
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------SKLEEEV-SRIEARLREIEQKLNRLTLEkeYL 831
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  489 KERMAALEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 543
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
332-542 4.73e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 59.78  E-value: 4.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  332 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLp 411
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ- 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  412 evEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 473
Cdd:COG4942    103 --KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  474 DRLLTEsNERLQLHLKERMAALEEKNvliQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 542
Cdd:COG4942    181 AELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PRK01156 PRK01156
chromosome segregation protein; Provisional
35-485 4.74e-09

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 61.07  E-value: 4.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLTGSKGADPP 101
Cdd:PRK01156   244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKS 179
Cdd:PRK01156   324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKI 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  180 LFEHHKALDeKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNG 259
Cdd:PRK01156   400 QEIDPDAIK-KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHY 474
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  260 SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSrvGEVEQ------EAETARKDLIKTE-------EMNTKYQ--- 323
Cdd:PRK01156   475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLEDIKikinelkDKHDKYEeik 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  324 -----------RDIRECYLQAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDKLENELANKEA----ILRQMEEKNRQ 388
Cdd:PRK01156   553 nrykslkledlDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANN 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH 465
Cdd:PRK01156   631 LNNKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
                          490       500
                   ....*....|....*....|
gi 1720361586  466 NKRLSDTVdrllTESNERLQ 485
Cdd:PRK01156   711 INELSDRI----NDINETLE 726
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
902-968 5.11e-09

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: 53.84  E-value: 5.11e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586   902 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 968
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
255-543 5.85e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 5.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  255 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 334
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLE 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLelAEQKLQQTMRKAETLPEVE 414
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEV 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  415 AELAQRIAALTKAEERhgnieermRHLEGQ-LEEKNQELQrarqrEKMNEEHNKRlsdtvdrlltESNERLQLHLKERMA 493
Cdd:TIGR02169  808 SRIEARLREIEQKLNR--------LTLEKEyLEKEIQELQ-----EQRIDLKEQI----------KSIEKEIENLNGKKE 864
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720361586  494 ALEEKnvlIQESENFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 543
Cdd:TIGR02169  865 ELEEE---LEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
268-464 8.19e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.07  E-value: 8.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIrecylqaMAQKEDMEERITTL 347
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-------AEAEAEIEERREEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  348 EKRYLSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET 409
Cdd:COG3883     89 GERARALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEA 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  410 -LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 464
Cdd:COG3883    169 aKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
300-537 8.23e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 8.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  300 EVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA-MAQK-EDMEERITTLEKRYLSAQREStsihdmndkLENELANKEA 377
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILNELERQLKSLERQAeKAERyKELKAELRELELALLVLRLEE---------LREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  378 ILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEERmrhLEGQLEEKNQELQRARQ 457
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISR---LEQQKQILRERLANLER 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  458 REKMNE---EHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvlIQESENFRKNLEESLHDKErlaEEIEKLRSELD 534
Cdd:TIGR02168  317 QLEELEaqlEELESKLDELAEELAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVA 389

                   ...
gi 1720361586  535 QMK 537
Cdd:TIGR02168  390 QLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
265-689 9.48e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 9.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  265 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecYLQAMAQKEDMEERI 344
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER------------YQALLKEKREYEGYE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  345 TTLEKRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAAL 424
Cdd:TIGR02169  228 LLKEKEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVK 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  425 TKAEERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKRLSdtvdrlltesnerlqlhlkermaaleeknvliq 503
Cdd:TIGR02169  294 EKIGELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDKLLA--------------------------------- 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLieptisrthidtSTELRYSVGSLVDSQSDYRTTKVIRRPR 583
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINEL 404
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  584 RGRMGVRRDEPKVKS--LGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQL 661
Cdd:TIGR02169  405 KRELDRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEY 478
                          410       420
                   ....*....|....*....|....*...
gi 1720361586  662 DAINKEIRLIQEEKESTELRAEEIENRV 689
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
39-475 1.48e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLTGSKgadppEFAALTKELNACREQLL 118
Cdd:COG1196    385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-----ALEEAAEEEAELEEEEE 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  119 EKEEEISELKAERNNTRLLLEHLecLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLfehhKALDEKVRERLRVS 198
Cdd:COG1196    460 ALLELLAELLEEAALLEAALAEL--LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL----RGLAGAVAVLIGVE 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  199 LERVSALEEELAAANQEIVALREQN---------------VHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS 263
Cdd:COG1196    534 AAYEAALEAALAAALQNIVVEDDEVaaaaieylkaakagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDDTSQIVELQELLEKQNYEMAqmKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 343
Cdd:COG1196    614 RYYVLGDTLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 423
Cdd:COG1196    692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361586  424 LTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 475
Cdd:COG1196    772 LEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
169-513 2.53e-08

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 58.60  E-value: 2.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  169 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVS-------LERVSALEEELAAANQEIValREQNVHIQRKMVS 232
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMD--RQAAIYAEQERMA 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  233 SEGSTESEHLegmeagqKVHEKRLSNGSIDSTDDTSQIVELQELlEKQNYEMAQMKERltalssrvgeVEQEAETARKDL 312
Cdd:pfam17380  344 MERERELERI-------RQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVK 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  313 IKTEEMNTKYQRDIRECYL----QAMAQKEDM----EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 384
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQiraeQEEARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  385 KNRQLQERLELAEQKLQQtmRKAETLPE------VEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEknqelqRARQR 458
Cdd:pfam17380  486 RKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQE--MEE------RRRIQ 555
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  459 EKMneehnkrlsdtvdRLLTESNERLQLHLKERmaaleEKNVLIQESENFRKNLE 513
Cdd:pfam17380  556 EQM-------------RKATEERSRLEAMERER-----EMMRQIVESEKARAEYE 592
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-532 2.56e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   30 HFEQLM---VNMLDERDR--LLDTLRETQESLSLAQQRLQDVIYDRDSLQ----RQLNSALPQDIESLTGGLtgskgadp 100
Cdd:COG4913    233 HFDDLErahEALEDAREQieLLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAELEELRAEL-------- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  101 pefAALTKELNACREQLLEKEEEISELKAERNNTRL-LLEHLECLVSRHERSLRMTVVKRQAQS----------PSGVSS 169
Cdd:COG4913    305 ---ARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEallaalglplPASAEE 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  170 EVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE------QNVHIQRKMVSSE-GSTESE-- 240
Cdd:COG4913    382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipARLLALRDALAEAlGLDEAElp 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  241 -----------------HLEGMEAGQK----VHEKRLS--NGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTA--LS 295
Cdd:COG4913    462 fvgelievrpeeerwrgAIERVLGGFAltllVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAgkLD 541
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  296 SRVGEVEQEAE---TARKDLIK---TEEMN-----------TKYQRDIRECYLQAMAQKE-----DMEERITTLEKRYls 353
Cdd:COG4913    542 FKPHPFRAWLEaelGRRFDYVCvdsPEELRrhpraitragqVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAEL-- 619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  354 aqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEER 430
Cdd:COG4913    620 ------------AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDD 686
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  431 HGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQ 503
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERE 766
                          570       580
                   ....*....|....*....|....*....
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSE 532
Cdd:COG4913    767 LRENLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-431 3.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 3.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----LPQDIESLTGGLTG------SKGADP--PEFAALTKELN 111
Cdd:TIGR02168  181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykeLKAELRELELALLVlrleelREELEElqEELKEAEEELE 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  112 ACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKaldekv 191
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQK------ 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  192 rERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMVSSEgstesehlegmeagqkvhekrlsngsidstddtSQIV 271
Cdd:TIGR02168  305 -QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE---------------------------------EKLE 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTLEKRy 351
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE----RLEARLERLEDRRERLQQE- 422
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  352 LSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 431
Cdd:TIGR02168  423 IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
PTZ00121 PTZ00121
MAEBL; Provisional
30-548 3.67e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDiESLTGGLTGSKGADP----PEFAA 105
Cdd:PTZ00121  1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAakkkAEEAK 1342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEH--LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEH 183
Cdd:PTZ00121  1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  184 HKALDEKVRErlrvslervsalEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHL-EGMEAGQKVHEKRLSNGSID 262
Cdd:PTZ00121  1423 AKKKAEEKKK------------ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEAKK 1490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  263 STDDTSQIVE---LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIRECYLQAMAQK 337
Cdd:PTZ00121  1491 KAEEAKKKADeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAK 1570
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  338 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAE 408
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAE 1650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  409 TLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHL 488
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAE 1725
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  489 KERMAALEEknvLIQESENFRKNLEESLHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 548
Cdd:PTZ00121  1726 EENKIKAEE---AKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
30-496 4.10e-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: 57.82  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN--SALPQDIESLTGGLTGS---- 95
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrNMEVQRLEALLKAMKSEcqgq 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   96 ----------KGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 165
Cdd:pfam15921  446 merqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  166 GVSSEVEVLKALKSLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMVSSEGSTESE-HLEG 244
Cdd:pfam15921  525 RVDLKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQ-IENMTQLVGQHGRTAGAmQVEK 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  245 MEAGQKVHEKRLSNGSIDSTDDT--SQIVELQELLEKQNYEMAQM----KERLTALSSRVGEVEQ---EAETARKDLIKT 315
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKILKDKkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSL 672
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  316 EEMNTKYQRDIREcylqamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ--- 388
Cdd:pfam15921  673 SEDYEVLKRNFRN-------KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQida 745
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  389 LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkR 468
Cdd:pfam15921  746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------Q 819
                          490       500
                   ....*....|....*....|....*...
gi 1720361586  469 LSDTVDRLLTESNERLQLHLKERMAALE 496
Cdd:pfam15921  820 FAECQDIIQRQEQESVRLKLQHTLDVKE 847
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
186-534 4.72e-08

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: 57.65  E-value: 4.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQ------RKMVSSEGSTESEHLEgmeagQKVHEKRlsng 259
Cdd:COG3096    829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllNKLLPQANLLADETLA-----DRLEELR---- 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  260 sidstddtsqiVELQELLEKQNYeMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMntkyQRDirecYLQAMAQKED 339
Cdd:COG3096    900 -----------EELDAAQEAQAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQL----QAD----YLQAKEQQRR 952
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  340 MEERITTLEkrYLSAQRESTSIHD----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET 409
Cdd:COG3096    953 LKQQIFALS--EVVQRRPHFSYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA 1030
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  410 LPEVEAELAQRIAAL-----TKAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTE 479
Cdd:COG3096   1031 KQQTLQELEQELEELgvqadAEAEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQ 1105
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  480 SNERLQLHLKERMAALEeknvLIQESenfrkNLEESLHDKERLAEEIEKLRSELD 534
Cdd:COG3096   1106 EREQVVQAKAGWCAVLR----LARDN-----DVERRLHRRELAYLSADELRSMSD 1151
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-544 4.73e-08

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: 57.72  E-value: 4.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 185
Cdd:TIGR04523  171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMV--SSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS 263
Cdd:TIGR04523  233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDDTSQivELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqamaqKEDMEER 343
Cdd:TIGR04523  305 EQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE--------KQNEIEK 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 IttlekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 423
Cdd:TIGR04523  375 L----------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  424 LTKA----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlq 485
Cdd:TIGR04523  445 LTNQdsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS--- 521
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  486 lhLKERMAALE----EKNVLIQESENFRKNLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 544
Cdd:TIGR04523  522 --LKEKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
115-524 4.83e-08

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: 57.75  E-value: 4.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  115 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 189
Cdd:TIGR00606  684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  190 KVrERLRVSLERVSAL------EEELAAANQEIVALREQnVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS 263
Cdd:TIGR00606  759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDDT--SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIRECYLQAMAQKEDME 341
Cdd:TIGR00606  837 ELDTvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST----EVQSLIREIKDAKEQDS 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 421
Cdd:TIGR00606  913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  422 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 498
Cdd:TIGR00606  984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1720361586  499 NVLIQESENF-----RKNLEESLHDKERLAE 524
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELRE 1093
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
268-534 5.05e-08

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 56.61  E-value: 5.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqRDIRECYLQAMAQKEDMEER---I 344
Cdd:pfam19220   48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE-------AALREAEAAKEELRIELRDKtaqA 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  345 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 424
Cdd:pfam19220  121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  425 TKAEERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQ 503
Cdd:pfam19220  201 ETQLDAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLA 265
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSELD 534
Cdd:pfam19220  266 EARNQLRDRDEAIRAAERRLKEASIERDTLE 296
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
262-540 7.35e-08

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: 57.11  E-value: 7.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  262 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDI---RECYLQAMAQKE 338
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLeseRAARNKAEKQRR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  339 DMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENELANKEAILRQMEEKNRQ----LQERLELAEQKLQQ 402
Cdd:pfam01576  296 DLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKAN 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  403 TMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNK-------------- 467
Cdd:pfam01576  375 LEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQELQARLSESeRQRAELAEKLSKlqselesvssllne 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  468 ------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEknvliqESENFRKNLEESLHDKERLAEEIEKLRSE 532
Cdd:pfam01576  452 aegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED------ERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525

                   ....*...
gi 1720361586  533 LDQMKMRT 540
Cdd:pfam01576  526 LSDMKKKL 533
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
36-498 7.39e-08

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: 57.04  E-value: 7.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRQLNS--ALPQDIESLTGGLtgskgadppefAALTKELNA 112
Cdd:pfam05483  270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTI-----------CQLTEEKEA 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  113 CREQLLEKEEE----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEH 183
Cdd:pfam05483  336 QMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEEL 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  184 HKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEK-RLSNG 259
Cdd:pfam05483  411 KKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeKLKNI 488
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  260 SI----------------DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-KTEEMNTKY 322
Cdd:pfam05483  489 ELtahcdklllenkeltqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqKGDEVKCKL 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  323 ------QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELANK 375
Cdd:pfam05483  569 dkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASA 648
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  376 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRHLe 442
Cdd:pfam05483  649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSEL- 727
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  443 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMAALEEK 498
Cdd:pfam05483  728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTAILKDK 786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
102-455 9.18e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 9.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERnntRLLLEHLEclvsRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLF 181
Cdd:COG1196    261 ELAELEAELEELRLELEELELELEEAQAEE---YELLAELA----RLEQDIARLEERRRELE----ERLEELEEELAELE 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRERlrvsLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRlsngsi 261
Cdd:COG1196    330 EELEELEEELEEL----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA------ 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  262 dstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNtkyqrdirecyLQAMAQKEDME 341
Cdd:COG1196    400 ------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-----------AELEEEEEALL 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQRI 421
Cdd:COG1196    463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAAL 540
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1720361586  422 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 455
Cdd:COG1196    541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1034-1089 1.12e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.12e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  1034 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
269-483 1.37e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.16  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLe 348
Cdd:COG4942     35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  349 krYLSAQRESTSI----HDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 424
Cdd:COG4942    114 --YRLGRQPPLALllspEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  425 TKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 483
Cdd:COG4942    191 EALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
192-531 1.39e-07

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: 56.11  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQR---KMVSSEGSTE------SEHLEGMEAGQKVHEKrlsngsID 262
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAReleELSARESDLEqdyqaaSDHLNLVQTALRQQEK------IE 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  263 STDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE------CYLQAMAQ 336
Cdd:COG3096    351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVqqtraiQYQQAVQA 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  337 KEDMEERittLEKRYLSAqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PE 412
Cdd:COG3096    422 LEKARAL---CGLPDLTP-----------ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGE 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  413 VEAELA-QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKER 491
Cdd:COG3096    488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAEL 562
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720361586  492 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRS 531
Cdd:COG3096    563 EAQLEE---LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
354-534 2.11e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  354 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 433
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  434 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESENFRKNLE 513
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348
                          170       180
                   ....*....|....*....|.
gi 1720361586  514 ESLHDKERLAEEIEKLRSELD 534
Cdd:PRK02224   349 EDADDLEERAEELREEAAELE 369
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-543 2.36e-07

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: 55.51  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQDIESLTGGLTGSKgadppefaaltKELNA 112
Cdd:pfam15921  328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKRE-----------KELSL 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  113 CREQ---LLEKEE----EISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:pfam15921  396 EKEQnkrLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALREQ-NVHIQRKmvsSEGSTESEHLEGMEAGQK 250
Cdd:pfam15921  475 EMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRSRvDLKLQEL---QHLKNEGDHLRNVQTECE 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  251 VHEKRLSngsidstdDTSQIVE-LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREc 329
Cdd:pfam15921  552 ALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE- 622
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  330 yLQAMAQKEDMEE-RITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAE 408
Cdd:pfam15921  623 -LEARVSDLELEKvKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  409 T-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlh 487
Cdd:pfam15921  699 MqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN------ 761
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  488 lKERMAALEEKNVLIQEsenfrknLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 543
Cdd:pfam15921  762 -KEKHFLKEEKNKLSQE-------LSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
347-539 2.71e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 2.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 426
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  427 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 503
Cdd:COG4717    131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720361586  504 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:COG4717    200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
220-534 3.00e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.18  E-value: 3.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  220 REQNVHIQRKMVSSEGSTESEHLEGMEAG-QKVH-EKRLSNGSIDSTDDTSQIVELQEllEKQNYEMAQMKERLTALSSR 297
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  298 VGEVEQEAETARKDLIKTEEMNTKYQRDIRECylqamaqkedmEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 377
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKE-----------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  378 ILRQMEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK----- 448
Cdd:pfam01576  237 QLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldtta 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  449 -NQELQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI----- 502
Cdd:pfam01576  317 aQQELRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelr 394
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720361586  503 ------QESENFRKNLEESLHD-----------KERLAEEIEKLRSELD 534
Cdd:pfam01576  395 tlqqakQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELE 443
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
265-533 3.62e-07

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: 54.98  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  265 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE-QEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 343
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 421
Cdd:pfam02463  239 IDLLQELLRDEQEEIES---SKQEIEKEEEKLAQVLKENKEEEKekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  422 AA-----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 493
Cdd:pfam02463  316 LKesekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720361586  494 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 533
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
379-537 6.57e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 6.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  379 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQR 458
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  459 EKMNEEHNKRLSDTVDRL--------------LTESNERLQLH---LKERMAALEEKNVLIQESENFRKNLEESLHDKER 521
Cdd:COG4942     99 LEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERAELEA 178
                          170
                   ....*....|....*.
gi 1720361586  522 LAEEIEKLRSELDQMK 537
Cdd:COG4942    179 LLAELEEERAALEALK 194
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1112-1183 6.63e-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: 47.68  E-value: 6.63e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  1112 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1183
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
91-461 8.02e-07

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 53.15  E-value: 8.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   91 GLTGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspsgvssE 170
Cdd:pfam19220   73 GLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE---------------RQLAA-------E 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  171 VEVLKALKslfEHHKALdekvRERLRVSLERVSALEEELAAAnQEIVALREQNVHIQRKMVSSEGSTESEHlegmEAGQK 250
Cdd:pfam19220  131 TEQNRALE---EENKAL----REEAQAAEKALQRAEGELATA-RERLALLEQENRRLQALSEEQAAELAEL----TRRLA 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  251 VHEKRLSNGSIDSTDDTSQIVELQELLEK----QNYEMAQMKERLTALSSRVgeveqEAETARkdLIKTEEMNTkyqrdi 326
Cdd:pfam19220  199 ELETQLDATRARLRALEGQLAAEQAERERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA------ 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  327 recylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRK 406
Cdd:pfam19220  266 -----EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTK 332
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  407 AetlpeveaeLAQRIAALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 461
Cdd:pfam19220  333 A---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
PRK12704 PRK12704
phosphodiesterase; Provisional
371-528 9.02e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.24  E-value: 9.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  371 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 450
Cdd:PRK12704    34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  451 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 527
Cdd:PRK12704   111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179

                   .
gi 1720361586  528 K 528
Cdd:PRK12704   180 E 180
mukB PRK04863
chromosome partition protein MukB;
192-529 1.21e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.04  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRK---MVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDts 268
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL-------IKTEEMNTKYQ------RDIREC------ 329
Cdd:PRK04863   356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqalDVQQTRAIQYQqavqalERAKQLcglpdl 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  330 -------YL-QAMAQKEDMEERITTLEKRyLSAQRESTSIHD--------MNDKLENELANKEAI--------------- 378
Cdd:PRK04863   436 tadnaedWLeEFQAKEQEATEELLSLEQK-LSVAQAAHSQFEqayqlvrkIAGEVSRSEAWDVARellrrlreqrhlaeq 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  379 ----------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 448
Cdd:PRK04863   515 lqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  449 NQELQRARQrekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQESEnFRKNLEESLHDKERLAEEI 526
Cdd:PRK04863   595 IQRLAARAP-----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLERERE-LTVERDELAARKQALDEEI 661

                   ...
gi 1720361586  527 EKL 529
Cdd:PRK04863   662 ERL 664
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
105-538 1.42e-06

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: 52.87  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  105 ALTKELNACREQLLEKEEEISELKAERNNTRlllEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSevevlkaLKSLFE 182
Cdd:pfam01576  212 KLEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARleEETAQKNNALKKIRELEAQISE-------LQEDLE 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  183 HHKALDEKVRERLRVSLERVSALEEEL------AAANQEIVALREQNVHIQRKMVSSEGstesehlegmeagqKVHEKRL 256
Cdd:pfam01576  282 SERAARNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQL 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  257 SNGSIDSTddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIRECYLQamaq 336
Cdd:pfam01576  348 QEMRQKHT---QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQ---- 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  337 kedmeeritTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaE 416
Cdd:pfam01576  416 ---------ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---E 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  417 LAQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALE 496
Cdd:pfam01576  481 TRQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALE 544
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1720361586  497 E-KNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKM 538
Cdd:pfam01576  545 EgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
331-536 1.89e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.66  E-value: 1.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  331 LQAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK------L 400
Cdd:TIGR00618  183 LMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  401 QQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDRLL 477
Cdd:TIGR00618  263 KQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVKQQSSIEE 342
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  478 TESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH----DKERLAEEIEKLRSELDQM 536
Cdd:TIGR00618  343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-528 2.81e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 185
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQ--NVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRLSNGSIDS 263
Cdd:TIGR04523  307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisQLKKELTNSESENSEKQRELE-----EKQNEIEKLKKENQS 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  264 TDD-----TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE-----MNTKYQRDIRecYLQA 333
Cdd:TIGR04523  382 YKQeiknlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdlTNQDSVKELI--IKNL 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  334 MAQKEDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpev 413
Cdd:TIGR04523  460 DNTRESLETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL--- 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  414 EAELAQriaaltkaeerhgnIEERMRHLEGQLEEKNQELQRArQREKMNEEHNKRLsdtvdrlltesnERLQLHLKERMA 493
Cdd:TIGR04523  530 ESEKKE--------------KESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEI------------EELKQTQKSLKK 582
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1720361586  494 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 528
Cdd:TIGR04523  583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
190-537 2.87e-06

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: 51.39  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  190 KVRERLRVSLERVSALEEELAAANQEIVALREQNvHIQRKMVssegstesEHLEGM--EAGQKVHEKRLSNG-SIDSTDD 266
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE-EKNREEV--------EELKDKyrELRKTLLANRFSYGpAIDELEK 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 T-----SQIVELQELLEKQNYEMA-----QMKERLTALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIRECYLQAMAQ 336
Cdd:pfam06160  154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYREMEEE 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  337 KEDMEErittlekryLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAE 416
Cdd:pfam06160  227 GYALEH---------LNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAK 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  417 LaqriaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH-- 487
Cdd:pfam06160  287 K--------YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKev 357
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  488 ----LKERMAALEEKNVLIQES-ENFRKNLeESLHDKERLA-EEIEKLRSELDQMK 537
Cdd:pfam06160  358 ayseLQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
144-439 3.20e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  144 LVSRHERSLRMTVVKRQAQSPSGVSSEVEVLK-------ALKSL---------FEHHKALDEKVRERLRVSLERVSAL-- 205
Cdd:COG3206     60 LVEPQSSDVLLSGLSSLSASDSPLETQIEILKsrpvlerVVDKLnldedplgeEASREAAIERLRKNLTVEPVKGSNVie 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  206 ------EEELAA--ANQEIVALREQNvhIQRKMVSSEGSTE--SEHLEGM-----EAGQKVHEKRLSNGSIDSTDDT--- 267
Cdd:COG3206    140 isytspDPELAAavANALAEAYLEQN--LELRREEARKALEflEEQLPELrkeleEAEAALEEFRQKNGLVDLSEEAkll 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 -SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAetarkdlikTEEMNTKYQRDIRECYLQAMAQKEDMEERITT 346
Cdd:COG3206    218 lQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL---------PELLQSPVIQQLRAQLAELEAELAELSARYTP 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 426
Cdd:COG3206    289 NHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
                          330
                   ....*....|...
gi 1720361586  427 AEERHGNIEERMR 439
Cdd:COG3206    363 ARELYESLLQRLE 375
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
269-539 3.57e-06

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNYEMAQMKERLTALssrvgeVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLE 348
Cdd:pfam13868   81 QIEEREQKRQEEYEEKLQEREQMDEI------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  349 KRYLSAQREstsihdMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 428
Cdd:pfam13868  155 ERILEYLKE------KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  429 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQESE-N 507
Cdd:pfam13868  229 KKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEEREeQ 305
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1720361586  508 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:pfam13868  306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
332-506 3.66e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  332 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAilrQMEEKNRQLQERLELAEQKLQQTMRKAETLP 411
Cdd:COG3883     27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGERARALYRSGGSVS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  412 EVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 483
Cdd:COG3883    104 YLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
                          170       180
                   ....*....|....*....|...
gi 1720361586  484 LQLHLKERMAALEEKNVLIQESE 506
Cdd:COG3883    184 LAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-539 3.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  192 RERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehLEGMEAGQKVHEK--RLSNGSIDSTDDTSQ 269
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAE-------------------LDALQERREALQRlaEYSWDEIDVASAERE 669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  270 IVELQ---ELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITT 346
Cdd:COG4913    670 IAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD----ELQDRLEAAEDLARL 745
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALT 425
Cdd:COG4913    746 ELRALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLP 815
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  426 KAEERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHL 488
Cdd:COG4913    816 EYLALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEA 888
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  489 KERMAA--LEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:COG4913    889 RPRPDPevREFRQELRAVTSGaSLFDEELSEARFAALKRLIERLRSEEEESDRR 942
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
45-542 3.95e-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: 51.36  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQDIESltgglTGSKGADPPEFAALT-------------- 107
Cdd:pfam10174   58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTT-----SPVDGEDKFSTPELTeenfrrlqseherq 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  108 -KELNACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQspsgvssEVEVLK 175
Cdd:pfam10174  129 aKELFLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLG-------HLEVLL 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  176 ALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALrEQNVH---IQRKMVSSEGSTES----EHLEGMEAg 248
Cdd:pfam10174  202 DQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL-ERNIRdleDEVQMLKTNGLLHTedreEEIKQMEV- 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  249 QKVHEKRLSNgSIDSTDD-----TSQIVELQ---ELLEKQNYEMAQ----MKERLTALSSRVGEVEQEAETARKDLIKTE 316
Cdd:pfam10174  280 YKSHSKFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  317 EMNTKYQRDIREC------------YLQAM-------------------AQKEDMEERITTLEKRYLSAQRESTSIHDMN 365
Cdd:pfam10174  359 SFLNKKTKQLQDLteekstlageirDLKDMldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL 438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  366 DKLENELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-------IEER 437
Cdd:pfam10174  439 TTLEEALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglkKDSK 518
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  438 MRHLEGQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVDRLLTESN------ERLQLHLKE-------- 490
Cdd:pfam10174  519 LKSLEIAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVARYKEESGkaqaevERLLGILREvenekndk 598
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  491 --RMAALEE-------------KNVLIQESENFRKN---LEESLHDK------------ERLAEEIEKLRSELDQMKMRT 540
Cdd:pfam10174  599 dkKIAELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnladnsqqlqlEELMGALEKTRQELDATKARL 678

                   ..
gi 1720361586  541 GS 542
Cdd:pfam10174  679 SS 680
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
174-699 4.17e-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: 51.27  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEhlegMEAGQKVHE 253
Cdd:pfam15921   87 VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE----LEAAKCLKE 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  254 KRLSNGSidstddtSQIVELQELLEKQNYEMAQMKERLTALSsrvgeveqeaETARKDLIKTEEMNTKYQRDIRECyLQA 333
Cdd:pfam15921  163 DMLEDSN-------TQIEQLRKMMLSHEGVLQEIRSILVDFE----------EASGKKIYEHDSMSTMHFRSLGSA-ISK 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  334 MAQKEDME-----ERITTLEKRYLSAQRESTS-----IHDMNDKLENELANKEAILRQMEEKN-------RQLQERLEL- 395
Cdd:pfam15921  225 ILRELDTEisylkGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAssarsqaNSIQSQLEIi 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  396 AEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDR 475
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  476 LLT-------------ESNERL-------QLHLKERMAALEEKNVLIQESENFRKNLEE-----------SLHDKERLAE 524
Cdd:pfam15921  382 LLAdlhkrekelslekEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaAIQGKNESLE 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  525 EIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELRYS--VGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPK-VKSLGD 601
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGD 541
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  602 HEWNRTQQIGVLGSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTE 679
Cdd:pfam15921  542 HLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKD 617
                          570       580
                   ....*....|....*....|
gi 1720361586  680 LRAEEIENRVASVSLEGLNL 699
Cdd:pfam15921  618 AKIRELEARVSDLELEKVKL 637
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
269-447 5.12e-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: 49.15  E-value: 5.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAmaqkEDMEERITTLE 348
Cdd:COG1579      8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  349 KR---------YLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQ 419
Cdd:COG1579     80 EQlgnvrnnkeYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDE 149
                          170       180
                   ....*....|....*....|....*...
gi 1720361586  420 RIAALTKAEERhgnIEERMRHLEGQLEE 447
Cdd:COG1579    150 ELAELEAELEE---LEAEREELAAKIPP 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
268-551 7.51e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 7.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTL 347
Cdd:COG4372     45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE----SLQEEAEELQEELEEL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  348 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKA 427
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  428 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEN 507
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720361586  508 FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 551
Cdd:COG4372    272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
102-608 7.77e-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: 50.61  E-value: 7.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128  280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  171 VEVL-KALKSLFEHHKALDEKV-RERLRVSLE---RVSALEEELAAANQEIVALREqnvhiqrkmvssegsTESEHLEGM 245
Cdd:pfam12128  356 LENLeERLKALTGKHQDVTAKYnRRRSKIKEQnnrDIAGIKDKLAKIREARDRQLA---------------VAEDDLQAL 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  246 EAG-QKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmAQMKERLTALSSRVGEV--EQEAETARKDLIKTEEMNTKY 322
Cdd:pfam12128  421 ESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAreEQEAANAEVERLQSELRQARK 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  323 QRDIRECYLQAMAQKedMEERITTLEKRYLSAQRESTSIH-----DMNDKLEN--ELANKEAILR---QMEEKNRQLQER 392
Cdd:pfam12128  500 RRDQASEALRQASRR--LEERQSALDELELQLFPQAGTLLhflrkEAPDWEQSigKVISPELLHRtdlDPEVWDGSVGGE 577
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  393 LELAEQKLQ----QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 468
Cdd:pfam12128  578 LNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  469 LSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESENF-----RKNLEESLHDKERLAEEIEKLRSELDQMKmr 539
Cdd:pfam12128  658 LFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK-- 735
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361586  540 TGSLIEPTISRTHIDT-STELRYSVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 608
Cdd:pfam12128  736 AAIAARRSGAKAELKAlETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1034-1085 8.25e-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: 8.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720361586 1034 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1085
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-539 1.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  338 EDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 411
Cdd:COG4913    245 EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARLEAELERLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  412 EVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKER 491
Cdd:COG4913    316 ARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1720361586  492 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:COG4913    390 AALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
41-537 1.19e-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: 49.97  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQ---LNSALPQDIESltggltgskgADPPEFAALTKEL----NAC 113
Cdd:TIGR00618  308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrlLQTLHSQEIHI----------RDAHEVATSIREIscqqHTL 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  114 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE-RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR 192
Cdd:TIGR00618  378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  193 ERLRVSLERvSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNgsidSTDDTSQIVE 272
Cdd:TIGR00618  458 KIHLQESAQ-SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQR 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  273 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIK--------TEEMN--TKYQRDIREcYLQAMAQKEDMEE 342
Cdd:TIGR00618  533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqcdnrsKEDIPnlQNITVRLQD-LTEKLSEAEDMLA 611
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  343 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtMRKAETLPEVEAELAQRIA 422
Cdd:TIGR00618  612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP-KELLASRQLALQKMQSEKE 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  423 ALTKAEERHGNIEERMRHLEGQLEEKNQELQR------------ARQREKMNEEHNK--RLSDTVDRLLTESNERLQLHL 488
Cdd:TIGR00618  691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassslgsdlAAREDALNQSLKElmHQARTVLKARTEAHFNNNEEV 770
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1720361586  489 KERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:TIGR00618  771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
382-535 1.26e-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: 48.00  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  382 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 457
Cdd:COG1579      2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  458 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLH 517
Cdd:COG1579     81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156
                          170
                   ....*....|....*...
gi 1720361586  518 DKERLAEEIEKLRSELDQ 535
Cdd:COG1579    157 ELEELEAEREELAAKIPP 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
341-497 1.34e-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: 48.00  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  341 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqKLQQTMRKAETLPEVEAeLAQR 420
Cdd:COG1579     23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEA-LQKE 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  421 IAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 497
Cdd:COG1579     98 IESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-387 1.37e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LTGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR- 192
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAk 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  193 --ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKV--HEKRLSNGSIDSTDDTS 268
Cdd:TIGR02169  327 leAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKLKREINELKR 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDlIKTEEMNTKYQRDIRECYLQamaQKEDMEERITTLE 348
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQ---ELYDLKEEYDRVE 482
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1720361586  349 KRYLSAQREstsihdmndkleneLANKEAILRQMEEKNR 387
Cdd:TIGR02169  483 KELSKLQRE--------------LAEAEAQARASEERVR 507
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
267-560 1.54e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 TSQIVELQELLEKQNYEMAQMKERLTALS--SRVGEVEQEAETARKDLIKTEEMntkyqrdiRECYLQAMAQKEDMEERI 344
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE--------LERLDASSDDLAALEEQL 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  345 TTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAAL 424
Cdd:COG4913    695 EELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA 758
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  425 tKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAALEE 497
Cdd:COG4913    759 -LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEYEE 834
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  498 K--NVLIQESENFRKNLEESLHDKERLAEE-IEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 560
Cdd:COG4913    835 RfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
198-406 1.72e-05

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.82  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  198 SLERVSALEEELAAANQEIVALREQNVHIQRKmvssegstesehlegmeagQKVHEKRLSNgsIDSTDDtsqivELQELL 277
Cdd:pfam15619    9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  278 EKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKRYLSAQRE 357
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSED---KNLAEREELQKKLEQLEAKLEDKDEK 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  358 stsIHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 406
Cdd:pfam15619  140 ---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-426 1.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLTGSKGadppEFAALTKELNACREQLL 118
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELE 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  119 EKEEEISELKAERNNTR--LLLEHLECLVSRHERSLRM--TVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALdekVRER 194
Cdd:COG4717    217 EAQEELEELEEELEQLEneLEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALL---FLLL 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  195 LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTEsehlEGMEAGQKVHEKRLSNGSIDSTDDTSQIV--- 271
Cdd:COG4717    294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE----ELLELLDRIEELQELLREAEELEEELQLEele 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 -ELQELLEKQN-------YEMAQMKERLTALSSRVGEVEQEAETARKDLIktEEMNTKYQRDIRECYLQAMAQKEDMEER 343
Cdd:COG4717    370 qEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELE--ELLEALDEEELEEELEELEEELEELEEE 447
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQREstsIHDMNDklENELANKEAILRQMEEKNRQLQER---LELAEQKLQQTMRKA--ETLPEVEAELA 418
Cdd:COG4717    448 LEELREELAELEAE---LEQLEE--DGELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYreERLPPVLERAS 522

                   ....*...
gi 1720361586  419 QRIAALTK 426
Cdd:COG4717    523 EYFSRLTD 530
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
365-469 2.52e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  365 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGNIEERMR 439
Cdd:PRK00409   515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADEIIKELR 594
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720361586  440 HLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 469
Cdd:PRK00409   595 QLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-545 2.62e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  368 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 447
Cdd:PRK03918   174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  448 KNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQlHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIE 527
Cdd:PRK03918   254 KRKLEEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
                          170
                   ....*....|....*...
gi 1720361586  528 KLRSELDQMKMRTGSLIE 545
Cdd:PRK03918   328 ERIKELEEKEERLEELKK 345
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-537 2.78e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgvssevevlkaLKSLF 181
Cdd:COG4717     82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE----------------LAELP 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  182 EHHKALDEKVRERLRVsLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehlegmeagqkvhekrlsngsi 261
Cdd:COG4717    146 ERLEELEERLEELREL-EEELEELEAELAELQEELEELLEQ--------------------------------------- 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  262 DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDME 341
Cdd:COG4717    186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERITTLEKRYLSAQRESTSIHDMndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA----EL 417
Cdd:COG4717    266 GSLLSLILTIAGVLFLVLGLLAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeellEL 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  418 AQRIAALTKAEERHGNIEERMRhLEGQLEEKNQELQRA--------RQREKMNEEHNKRLsdtvdRLLTESNERLQLHLK 489
Cdd:COG4717    343 LDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAgvedeeelRAALEQAEEYQELK-----EELEELEEQLEELLG 416
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720361586  490 ERMAALE--EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:COG4717    417 ELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
369-535 3.09e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 3.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  369 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 448
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  449 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesenfRKNLEESLHDKER 521
Cdd:COG3883     92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
                          170
                   ....*....|....
gi 1720361586  522 LAEEIEKLRSELDQ 535
Cdd:COG3883    162 LKAELEAAKAELEA 175
PTZ00121 PTZ00121
MAEBL; Provisional
181-532 3.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  181 FEHHKALDEKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGS 260
Cdd:PTZ00121  1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED---ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  261 iDSTDDTSQIVELQELLE-KQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIRECYLQAMAQKED 339
Cdd:PTZ00121  1170 -RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARK---AEDAKKAEAVKKAEEAKKDAEEAKKA 1245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  340 MEERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 419
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  420 RIAALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE-RLQLHLKERMAAL 495
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEED 1403
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1720361586  496 EEKNVLIQESENFRKNLEESLHDKE--RLAEEIEKLRSE 532
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-545 3.88e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  173 VLKALKSLFEhhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVH 252
Cdd:COG4717     39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEEL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  253 EKRLsngsidstDDTSQIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQ 332
Cdd:COG4717    115 REEL--------EKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  333 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ----------- 401
Cdd:COG4717    183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallall 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  402 ----------------------------QTMRKAETLPEVEAELAQRIAALTKAEE--------RHGNIEERMRHLEGQL 445
Cdd:COG4717    263 glggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEeeleellaALGLPPDLSPEELLEL 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  446 EEKNQELQRA-RQREKMNEEHN-KRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQESENFRKNLEESL 516
Cdd:COG4717    343 LDRIEELQELlREAEELEEELQlEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1720361586  517 --HDKERLAEEIEKLRSELDQMKMRTGSLIE 545
Cdd:COG4717    423 eaLDEEELEEELEELEEELEELEEELEELRE 453
COG5022 COG5022
Myosin heavy chain [General function prediction only];
309-532 5.43e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.77  E-value: 5.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  309 RKDLIKTEEMNTKYQRDI-RECYLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndklenelanKEAILRQMEEKNR 387
Cdd:COG5022    809 RKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRSLKAK-----------------KRFSLLKKETIYL 871
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  388 QLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQRE 459
Cdd:COG5022    872 QSAQRVELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYV 951
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  460 KmNEEHNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSE 532
Cdd:COG5022    952 K-LPELNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
422-537 5.71e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  422 AALTKAEERHGNIEER-----MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLK-----ER 491
Cdd:COG2433    380 EALEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSearseER 458
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1720361586  492 MAALEEKNVLIQESENfrKNLEESLHDKErlaEEIEKLRSELDQMK 537
Cdd:COG2433    459 REIRKDREISRLDREI--ERLERELEEER---ERIEELKRKLERLK 499
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
186-533 5.82e-05

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: 47.53  E-value: 5.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLE-GMEAGQKVHEKRLSNGSIDST 264
Cdd:pfam12128  597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKALAER 676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  265 DDTSQI------VELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIRecylqama 335
Cdd:pfam12128  677 KDSANErlnsleAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAKAE-------- 748
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  336 QKEDMEERITTLEKRYLSAQRE---STSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LP 411
Cdd:pfam12128  749 LKALETWYKRDLASLGVDPDVIaklKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaIS 824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  412 EVEAELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKE 490
Cdd:pfam12128  825 ELQQQLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGE 890
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1720361586  491 RMAALEE-KNVLIQESENFRKNLEE-----SLHDKERLAEEIEKLRSEL 533
Cdd:pfam12128  891 RLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
268-430 6.98e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  268 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK-------DLIKTEEMNTKYQ------RDIREcYLQAM 334
Cdd:COG1579     17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeikrlelEIEEVEARIKKYEeqlgnvRNNKE-YEALQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDMEERITTLEKRYLsaqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVE 414
Cdd:COG1579     96 KEIESLKRRISDLEDEIL--------------ELMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAELE 159
                          170
                   ....*....|....*.
gi 1720361586  415 AELAQRIAALTKAEER 430
Cdd:COG1579    160 ELEAEREELAAKIPPE 175
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
244-537 7.49e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  244 GMEAGQKVHEKRLSNGSIdSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 323
Cdd:COG4372      1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  324 RDIRecylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 403
Cdd:COG4372     80 EELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  404 MRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 483
Cdd:COG4372    156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  484 LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:COG4372    236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
PRK11281 PRK11281
mechanosensitive channel MscK;
337-543 1.00e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.83  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  337 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 415
Cdd:PRK11281    38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  416 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 493
Cdd:PRK11281   113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  494 ALEEKNVLIQESENFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 543
Cdd:PRK11281   164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
904-968 1.20e-04

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: 41.10  E-value: 1.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  904 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 968
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
PRK12705 PRK12705
hypothetical protein; Provisional
387-584 1.36e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.24  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  387 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 466
Cdd:PRK12705    26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  467 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 539
Cdd:PRK12705    98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720361586  540 TGSLIEPTISRTHIDTSTELRYSVgslVDSQSDYRTTKVIRRPRR 584
Cdd:PRK12705   178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1112-1182 1.41e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.41e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586 1112 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1182
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
272-542 1.67e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.72  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITT 346
Cdd:COG5185    272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 412
Cdd:COG5185    352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  413 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 488
Cdd:COG5185    432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  489 KERMAALEEKNVLIQESENFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 542
Cdd:COG5185    509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
193-612 2.46e-04

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


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 45.50  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  193 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEK--RLSNGSID----STDD 266
Cdd:COG5192    363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 TSQIVELQELLEKQNYEMAQMKERLTALS-SRVGEVEQE---AETARKDLIKTEemNTKYQRDIREC-YLQAMAQKEDME 341
Cdd:COG5192    440 ENEDVDFTGKKGAINNEDESDNEEVAFDSdSQFDESEGNlrwKEGLASKLAYSQ--SGKRGRNIQKIfYDESLSPEECIE 517
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  342 ERittlekrylsaQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQr 420
Cdd:COG5192    518 EY-----------KGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK- 582
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  421 iAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-- 498
Cdd:COG5192    583 -DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElr 654
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  499 -NVLIQESENFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGSLIEPTISRTHIDTSTELRYS----V 563
Cdd:COG5192    655 gNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHVPLEFVDEFNSRypivL 734
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720361586  564 GSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 612
Cdd:COG5192    735 GGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
367-537 2.83e-04

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: 43.76  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  367 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 446
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  447 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESENFRKNLEESL-HDKERLAE 524
Cdd:COG1579     84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149
                          170
                   ....*....|...
gi 1720361586  525 EIEKLRSELDQMK 537
Cdd:COG1579    150 ELAELEAELEELE 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
104-370 2.86e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 176
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  177 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEHLEGM--EAGQKVHEK 254
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR----LEAAEDLARLELRALLEERfaAALGDAVER 765
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  255 RLSNGSIDSTDD-TSQIVELQELLEKQnyeMAQMKERLTALSSRVG-EVEQEAETARK-DLIKTEEMnTKYQRDIREcyl 331
Cdd:COG4913    766 ELRENLEERIDAlRARLNRAEEELERA---MRAFNREWPAETADLDaDLESLPEYLALlDRLEEDGL-PEYEERFKE--- 838
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720361586  332 qamAQKEDMEERITTLeKRYLSAQRES--TSIHDMNDKLEN 370
Cdd:COG4913    839 ---LLNENSIEFVADL-LSKLRRAIREikERIDPLNDSLKR 875
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
272-458 2.99e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 45.07  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 ELQELLEKQNyEMAQMKERLT-------ALSSRVGEVEQ-EAEtaRKDLIKTEEMntkyQRDIRECYlQAMAQKED-MEE 342
Cdd:COG0497    173 ELEELRADEA-ERARELDLLRfqleeleAAALQPGEEEElEEE--RRRLSNAEKL----REALQEAL-EALSGGEGgALD 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  343 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPE 412
Cdd:COG0497    245 LLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLA 324
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720361586  413 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 458
Cdd:COG0497    325 YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
100-240 4.10e-04

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: 43.37  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  100 PPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKS 179
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRIS 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720361586  180 LFEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESE 240
Cdd:COG1579    107 DLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
309-536 4.35e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  309 RKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYlsaQRESTSIHDMND---KLENELANKEAILRQMEEK 385
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQKrirLLEKREAEAEEALREQAEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  386 NRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRARQR------- 458
Cdd:pfam05557   78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEELQERldllkak 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  459 ----EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESENFRKNLEESLHD 518
Cdd:pfam05557  148 aseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENIEN 222
                          250
                   ....*....|....*...
gi 1720361586  519 KERLAEEIEKLRSELDQM 536
Cdd:pfam05557  223 KLLLKEEVEDLKRKLERE 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
172-350 4.41e-04

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: 43.37  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  172 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLEGMEAGQKV 251
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  252 HEKRLsnGSIDSTDdtsqivELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYL 331
Cdd:COG1579     78 YEEQL--GNVRNNK------EYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
                          170
                   ....*....|....*....
gi 1720361586  332 QAMAQKEDMEERITTLEKR 350
Cdd:COG1579    146 ELDEELAELEAELEELEAE 164
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
390-528 4.98e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 41.52  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  390 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 469
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  470 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 528
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
905-963 5.04e-04

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 40.01  E-value: 5.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720361586  905 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 963
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
272-504 5.28e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 43.17  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYlQAMAQKEDMEERITTLEKR- 350
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAK-ELAEAIKNLIDNIKEINEKv 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  351 -YLSAQRESTSihdmNDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAee 429
Cdd:pfam06008  106 aTLGENDFALP----SSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA-- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  430 rhgnIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKN 499
Cdd:pfam06008  174 ----LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAAN 249

                   ....*
gi 1720361586  500 VLIQE 504
Cdd:pfam06008  250 LLLQE 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
114-394 5.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  114 REQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKvRE 193
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALE----AELDALQ-----ERREALQRLAEYSWDEIDVASAEREIAELEAE-LE 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  194 RLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNGSIDSTDDTSQivEL 273
Cdd:COG4913    679 RLDASSDDLAALEEQLEELEAELEELEEE----LDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRA--LL 751
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  274 QELLEKQNYEmAQMKERLTALSSRVGEVEQEAETARKDLIKTeeMNTkYQRDIRECYLQAMAQKEDMEE---RITTLEKR 350
Cdd:COG4913    752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA--MRA-FNREWPAETADLDADLESLPEylaLLDRLEED 827
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1720361586  351 YLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 394
Cdd:COG4913    828 GLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
193-556 5.40e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  193 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstESEHLEGMEAGQKVHEKRLSNgsidstddtsQIVE 272
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE---EQLKKQQLLKQLRARIEELRA----------QEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  273 LQELLEKQNYemAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIRECYLQAMAQKEDMEERITTLEkryl 352
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK----LLMKRAAHVKQQSSIEEQRRLLQ---- 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  353 SAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAaltkaeer 430
Cdd:TIGR00618  349 TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS-------- 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  431 hgnieeRMRHLEGQLeeknqelQRARQREKMNEEHNkrlsdtvdrlltesnERLQLHLKERMAALEEKNVLIQESENFRK 510
Cdd:TIGR00618  418 ------AFRDLQGQL-------AHAKKQQELQQRYA---------------ELCAAAITCTAQCEKLEKIHLQESAQSLK 469
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  511 NLEESLHDKERLAEEIEKLRSELDQMKMR--------TGSLIEPTISRTHIDTS 556
Cdd:TIGR00618  470 EREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplCGSCIHPNPARQDIDNP 523
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
299-554 6.67e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  299 GEVEQEAETARKDLIKTEE--MNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsihDMNDKLENELANKE 376
Cdd:pfam02463  142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-----KEQAKKALEYYQLK 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  377 AILRQMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLE 446
Cdd:pfam02463  217 EKLELEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEE 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  447 EKNQELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEI 526
Cdd:pfam02463  297 ELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
                          250       260
                   ....*....|....*....|....*...
gi 1720361586  527 EKLRSELDQMKMRTGSLIEPTISRTHID 554
Cdd:pfam02463  376 LAKKKLESERLSSAAKLKEEELELKSEE 403
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
152-695 6.79e-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: 44.27  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  152 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMV 231
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  232 SSEGSTESEHLEgmeagqkVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG------EVEQEA 305
Cdd:TIGR00606  294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  306 ETARKDLIKTEEMNTK---YQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 379
Cdd:TIGR00606  363 IRARDSLIQSLATRLEldgFERGPfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  380 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 459
Cdd:TIGR00606  443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  460 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF--RKNLEESLH----DKERLAEEIEKLRSEL 533
Cdd:TIGR00606  522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  534 DQMKMRTGSLIEPTISRTHIDTSTELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 611
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  612 VLGSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 691
Cdd:TIGR00606  681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755

                   ....
gi 1720361586  692 VSLE 695
Cdd:TIGR00606  756 VNRD 759
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
63-536 8.78e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 8.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   63 LQDVIYDRDSLQRQLNSALPQDIESLTGGLTGSKgadpPEFAALTKELNACRE---QLLEKEEEISELKAERNNT----R 135
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLE----EETAQKNNALKKIREleaQISELQEDLESERAARNKAekqrR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  136 LLLEHLECLVSRHERSLRMTVVKRQAQSPSgvSSEVEVLKalKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQE 215
Cdd:pfam01576  296 DLGEELEALKTELEDTLDTTAAQQELRSKR--EQEVTELK--KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  216 IV-------ALREQNVHIQRKMVS-SEGSTESEHlegmeaGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmaqm 287
Cdd:pfam01576  372 KAnlekakqALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE---- 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  288 kerLTALSSRVGEVEQEAETARKDLIKTEEMntkyQRDIRECYLQAMAQKEDMEERITTLEKrylsaqrESTSIHDMndk 367
Cdd:pfam01576  442 ---LESVSSLLNEAEGKNIKLSKDVSSLESQ----LQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ--- 504
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  368 LENELANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEG 443
Cdd:pfam01576  505 LEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQ 580
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  444 QLEEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLA 523
Cdd:pfam01576  581 ELDDLLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELE 656
                          490
                   ....*....|...
gi 1720361586  524 EEIEKLRSELDQM 536
Cdd:pfam01576  657 RTNKQLRAEMEDL 669
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
189-377 9.02e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMvssegSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTS 268
Cdd:COG4942     58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL-----EAQKEELAELLRALYRLGRQPPLALLLSPEDFL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDM----EERI 344
Cdd:COG4942    133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE----ALKAERQKLlarlEKEL 208
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720361586  345 TTLEKRYLSAQRESTSIHDMNDKLENELANKEA 377
Cdd:COG4942    209 AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
300-530 9.86e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 9.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  300 EVEQEAET-----ARKDLIKTEEMNTKYQRDIRECyLQAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMND 366
Cdd:PRK04778    90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDIEQI-LEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALD 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  367 KLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE----------- 429
Cdd:PRK04778   169 ELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyh 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  430 -RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQES 505
Cdd:PRK04778   249 lDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNS 312
                          250       260
                   ....*....|....*....|....*
gi 1720361586  506 ENFRKNLEESLHDKERLAEEIEKLR 530
Cdd:PRK04778   313 DTLPDFLEHAKEQNKELKEEIDRVK 337
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
174-411 1.11e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLEGMEAGQKVHE 253
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  254 KRLSNgSIDSTDDTSQIVELQELLEKQNyeMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQrdirecylqa 333
Cdd:COG4942    104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE---------- 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361586  334 mAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 411
Cdd:COG4942    171 -AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
41-290 1.30e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 42.75  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   41 ERDRLL---DTLRETQESLSLAQqrLQdviydrdslQRQLNSALPQDIESLTGGLTGSKGADPPEFaaltkelnacREQL 117
Cdd:pfam05622  226 EKERLIierDTLRETNEELRCAQ--LQ---------QAELSQADALLSPSSDPGDNLAAEIMPAEI----------REKL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  118 LEKEEEiselkaernNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRV 197
Cdd:pfam05622  285 IRLQHE---------NKMLRLGQEG--------------------------SYRERLTELQQLLEDANRRKNELETQNRL 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  198 SLERVSALE---EELAAANQEIVALREQNVHIQRKMvssegsteSEHLEG-MEAGQKVHEKRLSNGSIDSTDDTS---QI 270
Cdd:pfam05622  330 ANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKL--------EEHLEKlHEAQSELQKKKEQIEELEPKQDSNlaqKI 401
                          250       260
                   ....*....|....*....|
gi 1720361586  271 VELQELLEKQNYEMAQMKER 290
Cdd:pfam05622  402 DELQEALRKKDEDMKAMEER 421
Caldesmon pfam02029
Caldesmon;
192-532 1.34e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  192 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGM-EAGQKVHEKRLSngSIDSTDDTSQI 270
Cdd:pfam02029   12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFlDRTAKREERRQK--RLQEALERQKE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  271 VELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKR 350
Cdd:pfam02029   89 FDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  351 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALT 425
Cdd:pfam02029  169 VPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQ 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  426 KAEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQES 505
Cdd:pfam02029  249 KLEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQE 303
                          330       340
                   ....*....|....*....|....*..
gi 1720361586  506 ENFRKNLEEslHDKERLAEEIEKLRSE 532
Cdd:pfam02029  304 EAERKLREE--EEKRRMKEEIERRRAE 328
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
490-548 1.43e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.51  E-value: 1.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  490 ERMAALEEKNV-LIQESENFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 548
Cdd:PRK03992     1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
189-537 1.47e-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: 42.81  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHlEGMEAGQKVHEKRLSNGsiDSTDDTS 268
Cdd:pfam05557   44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLK--NELSELR 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQEL-LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA--MAQKEDMEE--- 342
Cdd:pfam05557  118 RQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdSEIVKNSKSela 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  343 RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------TM 404
Cdd:pfam05557  198 RIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglNL 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  405 RKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNERL 484
Cdd:pfam05557  276 RSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRRV 348
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  485 QLHLKERmaaleekNVLIQESENFRKNLEESLHDkERLAEEIEKLRSELDQMK 537
Cdd:pfam05557  349 LLLTKER-------DGYRAILESYDKELTMSNYS-PQLLERIEEAEDMTQKMQ 393
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
366-540 1.49e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  366 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 433
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  434 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 503
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720361586  504 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 540
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
287-537 1.51e-03

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: 42.79  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  287 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDME-------ERITTLEKRYL----SAQ 355
Cdd:pfam05483  160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhEKIQHLEEEYKkeinDKE 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  356 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERH 431
Cdd:pfam05483  240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDL 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  432 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESENF 508
Cdd:pfam05483  320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKF 399
                          250       260
                   ....*....|....*....|....*....
gi 1720361586  509 RKNLEESLHDKERLAEEIEKLRSELDQMK 537
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFE 428
Caldesmon pfam02029
Caldesmon;
187-493 1.52e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.55  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  187 LDEKVRERLRVSLERVSALEEELAAANqEIVALREQNVHIQRKmvssEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDD 266
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEK-ESVAERKENNEEEEN----SSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  267 TSQIVELQELLEKQNYEMAQMKERLTAlssRVGEVEQEAETARKDLIKTEEMNTKYQRDiRECYLQAMAQKEDMEERITT 346
Cdd:pfam02029  146 STEVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVFLDQK-RGHPEVKSQNGEEEVTKLKV 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  347 LEKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaalt 425
Cdd:pfam02029  222 TTKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL-------- 279
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361586  426 kaEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 493
Cdd:pfam02029  280 --EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
mukB PRK04863
chromosome partition protein MukB;
179-469 1.57e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  179 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHE 253
Cdd:PRK04863   797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA 876
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  254 KRLSNGSIDSTDDTSQIVELQELLEkQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMntkyqrdiRECYLQA 333
Cdd:PRK04863   877 LNRLLPRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL--------KQDYQQA 947
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  334 MAQKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMR 405
Cdd:PRK04863   948 QQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720361586  406 KAETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 469
Cdd:PRK04863  1028 SYDAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
114-452 1.62e-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: 42.89  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  114 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 185
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  186 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmvSSEGSTESEHLEGMEAG 248
Cdd:pfam10174  405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  249 QKVHEKRLSNGSIDSTDDTSQIVELQE--------------LLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK---- 310
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpei 556
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  311 -DLIKTEEMNTKYQRD-----------IRECYLQAMAQKEDMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAI 378
Cdd:pfam10174  557 nDRIRLLEQEVARYKEesgkaqaeverLLGILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGA 635
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720361586  379 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 452
Cdd:pfam10174  636 QLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
366-533 1.72e-03

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  366 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 434
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  435 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEn 507
Cdd:pfam04012  117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
                          170       180
                   ....*....|....*....|....*.
gi 1720361586  508 FRKNLEESLHDKERLAEEIEKLRSEL 533
Cdd:pfam04012  188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
273-539 1.76e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  273 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIRECYLQAMAQKEDMEErittLEKRYL 352
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEE----LEEKYK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  353 SAQRESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RH 431
Cdd:pfam07888  105 ELSASSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaER 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  432 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQES 505
Cdd:pfam07888  174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKV 253
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720361586  506 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 539
Cdd:pfam07888  254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
40-450 1.96e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586   40 DERDRLLDTLRETQEsLSLAQQRL-QDVIYDRDSLQRQLNsALPQ---------DIESLTGGLTGSKGAdppeFAALTKE 109
Cdd:COG3096    303 EEQYRLVEMARELEE-LSARESDLeQDYQAASDHLNLVQT-ALRQqekieryqeDLEELTERLEEQEEV----VEEAAEQ 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  110 LNACREQLLEKEEEISELKAErnntrlLLEHLECLVSRHERSLRMtvvkRQAqspsgvssevevLKALkslfehhkaldE 189
Cdd:COG3096    377 LAEAEARLEAAEEEVDSLKSQ------LADYQQALDVQQTRAIQY----QQA------------VQAL-----------E 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  190 KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgSTESEHLEGMEAGQKVhekrlsNGSIDSTDDTSQ 269
Cdd:COG3096    424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD-AARRQFEKAYELVCKI------AGEVERSQAWQT 496
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  270 IvelQELLEKQNYEMAQMkERLTALSSRVGEVEQ------EAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 343
Cdd:COG3096    497 A---RELLRRYRSQQALA-QRLQQLRAQLAELEQrlrqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ 572
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQREstsihdmndklENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTmrkaETLPEVEAELAQRIA 422
Cdd:COG3096    573 AAEAVEQRSELRQQ-----------LEQLRARIKELAARAPAWLAAQDALErLREQSGEAL----ADSQEVTAAMQQLLE 637
                          410       420
                   ....*....|....*....|....*...
gi 1720361586  423 ALTKAEERHGNIEERMRHLEGQLEEKNQ 450
Cdd:COG3096    638 REREATVERDELAARKQALESQIERLSQ 665
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
178-531 2.37e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 42.05  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  178 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMVSSEGSTESEHLEGMEAGQKVHEKR 255
Cdd:pfam09731  121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  256 LSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAE-TARKDLIKTEEMNTKYQRDIRECYLQAM 334
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELVSIFPDIIPVLKEDNL 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDME-------ERITTLEKR--------YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 399
Cdd:pfam09731  280 LSNDDLNsliahahREIDQLSKKlaelkkreEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  400 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRL 476
Cdd:pfam09731  358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK-LNEL 418
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  477 LTESNERLQLhLKERMAALEEKN---VLIQESENFRKNLEESLHDKER--LAEEIEKLRS 531
Cdd:pfam09731  419 LANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEALRSTLEDGSADSRPrpLVRELKALKE 477
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
202-534 2.50e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  202 VSALEEELAAANQEIVALREQnvhiqrkmvssegsteSEHLEGMEAGQKVHEKRLSngsidstDDTSQIVELQE------ 275
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQER----------------LDQLESGDDSGTPGGKKYL-------LLQKQLEQLQEenfrle 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  276 -----------LLEKQNYEMAQMKERLTAL-----------------SSRVGEVEQEAETARKdliKTEEMN-----TKY 322
Cdd:pfam05622   80 tarddyrikceELEKEVLELQHRNEELTSLaeeaqalkdemdilresSDKVKKLEATVETYKK---KLEDLGdlrrqVKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  323 QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQK 399
Cdd:pfam05622  157 LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQkekERLIIERDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  400 LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT-VDRLLT 478
Cdd:pfam05622  237 LRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAE--IREKLIRLQHENKMLRLGQEGSYRERLTeLQQLLE 314
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720361586  479 ESNER-----------------LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELD 534
Cdd:pfam05622  315 DANRRkneletqnrlanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1034-1089 2.57e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586 1034 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1089
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
379-492 2.99e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  379 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 457
Cdd:COG0542    413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  458 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 492
Cdd:COG0542    493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
246-419 3.15e-03

polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274386 [Multi-domain]  Cd Length: 498  Bit Score: 41.58  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  246 EAGQKVHEKRLSNG---SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-----KTEE 317
Cdd:TIGR03007  179 AAENRLKAFKQENGgilPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEA 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  318 MNTKYQrDIRECYLQAMAQKEDMEERITTLEKRYLSA-------QRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ 390
Cdd:TIGR03007  259 LEKQLD-ALRLRYTDKHPDVIATKREIAQLEEQKEEEgsaknggPERGEIANPVYQQLQIELAEAEAEIASLEARVAELT 337
                          170       180
                   ....*....|....*....|....*....
gi 1720361586  391 ERLElaeqklqQTMRKAETLPEVEAELAQ 419
Cdd:TIGR03007  338 ARIE-------RLESLLRTIPEVEAELTQ 359
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
277-472 3.31e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 40.66  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  277 LEKQNYEMAQMKERLTALSSRVGE-VEQEAETARKDLIKTEEMNtkyqrDIREcYLQAMAQK----EDMEERITTLEKRY 351
Cdd:cd07666     14 LTAQAWELSSHKKQGPGLLSRMGQtVKAVASSVRGVKNRPEEFT-----EMNE-YVEAFSQKinvlDKISQRIYKEQREY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  352 LSAQRESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAE 416
Cdd:cd07666     88 FEELKEYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAE 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720361586  417 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 472
Cdd:cd07666    165 LDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
280-514 3.59e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  280 QNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcyLQAMAQKEDMEERITTLEKRYLSAQREst 359
Cdd:COG3206    159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAE-- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  360 sihdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMR 439
Cdd:COG3206    235 -------------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720361586  440 HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 514
Cdd:COG3206    295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
189-435 3.65e-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: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  189 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehlegmeagqkvhekrlsngsidstddtS 268
Cdd:COG3883     26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  269 QIVELQELLEKQNyemAQMKERLTAL---SSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 343
Cdd:COG3883     73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESF-SDFLDRLSALSKIADADADLLEELKADKAELEAK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  344 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 423
Cdd:COG3883    149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
                          250
                   ....*....|..
gi 1720361586  424 LTKAEERHGNIE 435
Cdd:COG3883    229 AAAAAAAAAAAA 240
RNase_Y_N pfam12072
RNase Y N-terminal region;
387-527 3.87e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.87  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  387 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 450
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  451 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 527
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
177-452 4.02e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  177 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKrl 256
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  257 sngsidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETaRKDLIKTE-----EMNTKYQRDIRECYL 331
Cdd:pfam12128  337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIKEQnnrdiAGIKDKLAKIREARD 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  332 QAMAQKEDMEERITTLEKRYLSAQRESTSIhdmnDKLENELANKEAILRQ--------MEEKNRQLQERLELAEQKLQQT 403
Cdd:pfam12128  408 RQLAVAEDDLQALESELREQLEAGKLEFNE----EEYRLKSRLGELKLRLnqatatpeLLLQLENFDERIERAREEQEAA 483
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1720361586  404 MRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 452
Cdd:pfam12128  484 NAEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
318-537 4.16e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.21  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  318 MNTKYQRDIrecyLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAE 397
Cdd:COG0497    138 LDPDAQREL----LDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEA 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  398 QKLQqtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVD 474
Cdd:COG0497    201 AALQ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAE 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  475 RL------LTESNERLQLHLK------ERMAALEEK-----------NVLIQESENFRKNLEESLHDKERLAEEIEKLRS 531
Cdd:COG0497    269 RLesalieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEA 348

                   ....*.
gi 1720361586  532 ELDQMK 537
Cdd:COG0497    349 ELAEAE 354
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
274-456 4.26e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  274 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteEMNTKYQRDIRECylqamaqkEDMEERITTLEKRYLS 353
Cdd:cd00176     64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA--------DDLEQWLEEKEAALAS 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  354 aqrestsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGN 433
Cdd:cd00176    132 ------------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEE 190
                          170       180
                   ....*....|....*....|...
gi 1720361586  434 IEERMRHLEGQLEEKNQELQRAR 456
Cdd:cd00176    191 LNERWEELLELAEERQKKLEEAL 213
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
371-683 4.29e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  371 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 449
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  450 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVLIQ----ESENFRKNL--- 512
Cdd:pfam17380  360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEqiraEQEEARQREvrr 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  513 --EESLHDKERLAEE-------IEKLRSELDQMKMRTGSLIEPTISRTHIDtstELRYSVgslVDSQSDYRTTKVIRRPR 583
Cdd:pfam17380  440 leEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKI---LEKELEERKQAMIEEER 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  584 RGRMGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDA 663
Cdd:pfam17380  514 KRKLLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEA 570
                          330       340
                   ....*....|....*....|
gi 1720361586  664 INKEIRLIQEEKESTELRAE 683
Cdd:pfam17380  571 MEREREMMRQIVESEKARAE 590
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
259-446 4.82e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  259 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIrec 329
Cdd:cd22656     82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  330 ylqaMAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 407
Cdd:cd22656    152 ----EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLI 224
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720361586  408 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 446
Cdd:cd22656    225 ADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
910-967 5.55e-03

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: 36.45  E-value: 5.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361586  910 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 967
Cdd:cd09487      2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
272-469 7.17e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  272 ELQELLEKQNYEMAQMKERLTALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIREcylQAMAQKEDMEERITTLEKRY 351
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRRE---KQVIEKESRWREQAEDQENQ 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  352 LSAQRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAE 408
Cdd:pfam15558  107 RQEKLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVL 186
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  409 TLPEVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 469
Cdd:pfam15558  187 VDCQAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
172-429 7.56e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  172 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEeLAAANQEIVALREQNVHIQRkmvssegstESEHLEGMEAGQKV 251
Cdd:COG4913    222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  252 HEKRlsngsidstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQ---EAETARKDLIKTE-EMNTKYQRDIR 327
Cdd:COG4913    291 ELLE------------AELEELRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREiERLERELEERE 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  328 ECYLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 407
Cdd:COG4913    359 RRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
                          250       260
                   ....*....|....*....|..
gi 1720361586  408 ETLPEVEAELAQRIAALTKAEE 429
Cdd:COG4913    436 SNIPARLLALRDALAEALGLDE 457
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
1034-1078 8.40e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 8.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720361586 1034 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1078
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
mukB PRK04863
chromosome partition protein MukB;
104-456 8.69e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  104 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspsgvssevEVL 174
Cdd:PRK04863   782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELE 850
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  175 KALKSLFEHHKaldeKVRERLRVSLERVSALEEELAAANqeivaLREQNVHIQRKMVSSEGSTESEhlegmEAGQKV--H 252
Cdd:PRK04863   851 RALADHESQEQ----QQRSQLEQAKEGLSALNRLLPRLN-----LLADETLADRVEEIREQLDEAE-----EAKRFVqqH 916
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  253 EKRLSN-----GSIDStdDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEA-ETARKDLIKTEEMNTKyqrdI 326
Cdd:PRK04863   917 GNALAQlepivSVLQS--DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEK----L 990
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  327 RECYLQAMAQKEDMEERITTLE-------KRYLSAQRESTSIHDMNDKLENELankEAILRQMEEknrQLQERLELAEQK 399
Cdd:PRK04863   991 RQRLEQAEQERTRAREQLRQAQaqlaqynQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADS---GAEERARARRDE 1064
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720361586  400 LQQTMRKAETlpeveaelaqRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRAR 456
Cdd:PRK04863  1065 LHARLSANRS----------RRNQL---EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
PRK12705 PRK12705
hypothetical protein; Provisional
371-539 8.84e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  371 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 450
Cdd:PRK12705    40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  451 EL--QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENfRKNLEESLhdkERLAEEIEK 528
Cdd:PRK12705   120 ELeeLEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA-QNILAQAM---QRIASETAS 195
                          170
                   ....*....|....*..
gi 1720361586  529 LRS------ELDQMKMR 539
Cdd:PRK12705   196 DLSvsvvpiPSDAMKGR 212
PRK09039 PRK09039
peptidoglycan -binding protein;
335-456 9.11e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361586  335 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 414
Cdd:PRK09039    74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720361586  415 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 456
Cdd:PRK09039   147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
 
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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