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Conserved domains on  [gi|1327850359|ref|NP_001346607|]
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liprin-alpha-2 isoform 9 [Mus musculus]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1036-1107 2.20e-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: 154.40  E-value: 2.20e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1036 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1107
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 ...
 827-897 4.40e-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: 4.40e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  827 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 897
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 ...
 951-1016 1.05e-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: 1.05e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  951 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1016
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-465 5.39e-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: 80.49  E-value: 5.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  202 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 281
Cdd:TIGR02168  672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  282 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 357
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  358 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 431
Cdd:TIGR02168  817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1327850359  432 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 27-352 6.11e-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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 6.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSL 106
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDL---------------HKLEEALNDLEAR 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKAldEKVRERLRVSLERVSALEEELAAANQEIvalreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGS 186
Cdd:TIGR02169  788 LSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IdstddtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRdIRECYLQAMAQKEDM 266
Cdd:TIGR02169  861 G-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEK-KRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 346
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008


                   ....*.
gi 1327850359  347 IAALTK 352
Cdd:TIGR02169 1009 IEEYEK 1014
 
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 ...
 1036-1107 2.20e-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: 154.40  E-value: 2.20e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1036 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1107
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 ...
 827-897 4.40e-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: 4.40e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  827 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 897
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 ...
 951-1016 1.05e-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: 1.05e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  951 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1016
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-465 5.39e-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: 80.49  E-value: 5.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  202 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 281
Cdd:TIGR02168  672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  282 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 357
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  358 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 431
Cdd:TIGR02168  817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1327850359  432 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-471 1.68e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 1.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLrvslERVSALEEELAA-----ANQEIVALREQNVhiqrkmvssegSTESEHLEGMEAGQKVHEKRLsngsiDS 189
Cdd:COG1196    182 EATEENL----ERLEDILGELERqleplERQAEKAERYREL-----------KEELKELEAELLLLKLRELEA-----EL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  190 TDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqrdirecyLQAMAQKEDMEER 269
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------------YELLAELARLEQD 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  270 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAA 349
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEE 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  350 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQ 429
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEE 456

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1327850359  430 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 471
Cdd:COG1196    457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 950-1014 5.00e-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: 5.00e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  950 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-469 2.32e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 74.69  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 107
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  108 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI 187
Cdd:PRK02224   264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  188 DSTDDTSQIVELQEllekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDME 267
Cdd:PRK02224   336 AAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELE 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  268 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQ 345
Cdd:PRK02224   391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSP 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  346 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-E 422
Cdd:PRK02224   466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrE 544

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1327850359  423 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 469
Cdd:PRK02224   545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 827-893 4.03e-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: 4.03e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359   827 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 893
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 95-439 2.10e-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: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVS-------LERVSALEEELAAANQEIValREQNVHIQRKMVS 158
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMD--RQAAIYAEQERMA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  159 SEGSTESEHLegmeagqKVHEKRLSNGSIDSTDDTSQIVELQELlEKQNYEMAQMKERltalssrvgeVEQEAETARKDL 238
Cdd:pfam17380  344 MERERELERI-------RQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVK 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  239 IKTEEMNTKYQRDIRECYL----QAMAQKEDM----EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 310
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQiraeQEEARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  311 KNRQLQERLELAEQKLQQtmRKAETLPE------VEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEknqelqRARQR 384
Cdd:pfam17380  486 RKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQE--MEE------RRRIQ 555

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  385 EKMneehnkrlsdtvdRLLTESNERLQLHLKERmaaleEKNVLIQESENFRKNLE 439
Cdd:pfam17380  556 EQM-------------RKATEERSRLEAMERER-----EMMRQIVESEKARAEYE 592
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 959-1014 9.05e-08

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: 9.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359   959 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1037-1108 5.28e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 5.28e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  1037 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1108
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-352 6.11e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 6.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSL 106
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDL---------------HKLEEALNDLEAR 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKAldEKVRERLRVSLERVSALEEELAAANQEIvalreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGS 186
Cdd:TIGR02169  788 LSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IdstddtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRdIRECYLQAMAQKEDM 266
Cdd:TIGR02169  861 G-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEK-KRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 346
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008


                   ....*.
gi 1327850359  347 IAALTK 352
Cdd:TIGR02169 1009 IEEYEK 1014
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 829-893 1.01e-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: 41.49  E-value: 1.01e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  829 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 893
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1037-1107 1.20e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359 1037 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1107
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-296 2.00e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 102
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEHLEGM--EAGQKVHEK 180
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR----LEAAEDLARLELRALLEERfaAALGDAVER 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  181 RLSNGSIDSTDD-TSQIVELQELLEKQnyeMAQMKERLTALSSRVG-EVEQEAETARK-DLIKTEEMnTKYQRDIREcyl 257
Cdd:COG4913    766 ELRENLEERIDAlRARLNRAEEELERA---MRAFNREWPAETADLDaDLESLPEYLALlDRLEEDGL-PEYEERFKE--- 838

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1327850359  258 qamAQKEDMEERITTLeKRYLSAQRES--TSIHDMNDKLEN 296
Cdd:COG4913    839 ---LLNENSIEFVADL-LSKLRRAIREikERIDPLNDSLKR 875
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 292-466 7.08e-04

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: 42.43  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  292 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 359
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  360 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 429
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1327850359  430 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 466
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 95-216 1.82e-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: 42.37  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALE---EELAAANQEIVALREQNVHIQRKMvssegsteSEHLEG- 170
Cdd:pfam05622  301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKL--------EEHLEKl 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1327850359  171 MEAGQKVHEKRLSNGSIDSTDDTS---QIVELQELLEKQNYEMAQMKER 216
Cdd:pfam05622  373 HEAQSELQKKKEQIEELEPKQDSNlaqKIDELQEALRKKDEDMKAMEER 421
 
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 ...
 1036-1107 2.20e-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: 154.40  E-value: 2.20e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1036 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1107
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 ...
 827-897 4.40e-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: 4.40e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  827 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 897
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 ...
 951-1016 1.05e-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: 1.05e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  951 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1016
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 ...
 955-1014 1.78e-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: 1.78e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  955 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1014
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 ...
 834-892 3.02e-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: 3.02e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850359  834 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 892
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 ...
 1044-1105 5.89e-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: 5.89e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1044 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1105
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 ...
 1036-1107 1.25e-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: 1.25e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1036 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1107
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 ...
 828-892 3.89e-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: 3.89e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  828 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 892
Cdd:cd09564      2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 950-1014 1.31e-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: 75.04  E-value: 1.31e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  950 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 950-1014 1.49e-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: 75.14  E-value: 1.49e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  950 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1036-1107 1.95e-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: 1.95e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359 1036 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1107
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-465 5.39e-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: 80.49  E-value: 5.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  202 LLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAMAQKEDMEERITTLEKRYLSAQ 281
Cdd:TIGR02168  672 ILERRR-EIEELEEKIEELEEKIAELEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  282 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH---- 357
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtlln 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  358 ---GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMAALEEKNVLIQES 431
Cdd:TIGR02168  817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSEL 896

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1327850359  432 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-411 7.19e-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: 7.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKAL 103
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  104 KSLFEHHKALDEK---VRERLRVSLERVSALEEELAAANQEivaLREQNVHIQRKmvssegstesehlegmEAGQKVHEK 180
Cdd:TIGR02168  771 EEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAE---LTLLNEEAANL----------------RERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  181 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 260
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-----------ALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDMEERITTLEKRYLSAQresTSIHDMNDKLEnelankeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEV 339
Cdd:TIGR02168  901 EELRELESKRSELRRELEELR---EKLAQLELRLE-----------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDD 966

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  340 EAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLl 403
Cdd:TIGR02168  967 EEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV- 1041


                   ....*...
gi 1327850359  404 tesNERLQ 411
Cdd:TIGR02168 1042 ---NENFQ 1046
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-471 1.68e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 1.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLrvslERVSALEEELAA-----ANQEIVALREQNVhiqrkmvssegSTESEHLEGMEAGQKVHEKRLsngsiDS 189
Cdd:COG1196    182 EATEENL----ERLEDILGELERqleplERQAEKAERYREL-----------KEELKELEAELLLLKLRELEA-----EL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  190 TDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqrdirecyLQAMAQKEDMEER 269
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------------YELLAELARLEQD 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  270 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAA 349
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEE 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  350 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQ 429
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEE 456

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1327850359  430 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 471
Cdd:COG1196    457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-413 2.04e-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: 2.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   40 REQLLEKEEEISELKAERNNTRLLLEH-------LECLVSRHERSLRMtvVKRQAQspsgvssevevlKALKslfehHKA 112
Cdd:TIGR02168  157 RRAIFEEAAGISKYKERRKETERKLERtrenldrLEDILNELERQLKS--LERQAE------------KAER-----YKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  113 LDEKVRE-RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGS---TESEHLEgMEAGQKVHEKRLSNGSID 188
Cdd:TIGR02168  218 LKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE-LEEEIEELQKELYALANE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  189 STDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQrDIRECYLQAMAQKEDMEE 268
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---KLEELKEELE-SLEAELEELEAELEELES 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  269 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA--ETLPEVEAELAQR 346
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEEL 452

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  347 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 413
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-463 4.29e-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: 77.42  E-value: 4.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   40 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 119
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  120 RLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehLEGMEAgqKVHEKRLSNGSIDSTDDTSQIVEL 199
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEAR-------------------IEELEE--DLHKLEEALNDLEARLSHSRIPEI 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  200 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdliktEEMNTKyQRDIRECylqaMAQKEDMEERITTLEKRYls 279
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDL----KEQIKSIEKEIENLNGKK-- 863

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  280 aqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGN 359
Cdd:TIGR02169  864 ------------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEA 928

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  360 IEERMRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESENFR 435
Cdd:TIGR02169  929 LEEELSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVL 985

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1327850359  436 KNLEESLHDKERLAEE---IEKLRSELDQMK 463
Cdd:TIGR02169  986 KRLDELKEKRAKLEEErkaILERIEEYEKKK 1016
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 950-1014 5.00e-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: 5.00e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  950 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 108-423 1.55e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  108 EHHKALDEKVRER-LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRlsngs 186
Cdd:COG1196    213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 idstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqAMAQKEDM 266
Cdd:COG1196    288 -------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEA 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmRKAETLPEVEAELAQR 346
Cdd:COG1196    357 EAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE---RLERLEEELEELEEAL 430

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  347 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 423
Cdd:COG1196    431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-469 2.32e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 74.69  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 107
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  108 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSI 187
Cdd:PRK02224   264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  188 DSTDDTSQIVELQEllekqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylqamaQKEDME 267
Cdd:PRK02224   336 AAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRRE------------------EIEELE 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  268 ERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQ 345
Cdd:PRK02224   391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSP 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  346 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-E 422
Cdd:PRK02224   466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrE 544

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1327850359  423 EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 469
Cdd:PRK02224   545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-442 4.91e-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: 73.94  E-value: 4.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEG--STESEHLEGMEAGQKVHEKRLSNGSIDSTDD 192
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqiSALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqrdirecylqamAQKEDMEERITT 272
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------------------AELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTK 352
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----------ALLNERASLEEALAL 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  353 AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESE 432
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971

                          330
                   ....*....|
gi 1327850359  433 NFRKNLEESL 442
Cdd:TIGR02168  972 RRLKRLENKI 981
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-459 8.66e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.17  E-value: 8.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSL 106
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAE 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgsTESEHLEGMEAGQK--VHEKRLSN 184
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLS 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  185 GSIDS---------------------------TDDTSQIVELQELLEKQNYEMAQMKE----RLTALSSRVGEVEQEAET 233
Cdd:TIGR02168  520 GILGVlselisvdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEG 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  234 ARKDLIKTEEMNTKYQRDIRecYL-------------QAMAQKEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlE 295
Cdd:TIGR02168  600 FLGVAKDLVKFDPKLRKALS--YLlggvlvvddldnaLELAKKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-R 676

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  296 NELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQL 371
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKEL 756

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  372 EEKNQELQRARQREKMNEEHNKRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESENFRKNLEESLHD 444
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAA 835

                          490
                   ....*....|....*
gi 1327850359  445 KERLAEEIEKLRSEL 459
Cdd:TIGR02168  836 TERRLEDLEEQIEEL 850
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 827-891 1.21e-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: 1.21e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  827 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 891
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
30-461 3.17e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 3.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   30 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 106
Cdd:PRK03918   168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiQRKMVSSEGSTESEHLEgMEAGQKVHEKRLSNGS 186
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-----KVKELKELKEKAEEYIK-LSEFYEEYLDELREIE 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IDSTDDTSQIVELQEL---LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQR-------DIRECY 256
Cdd:PRK03918   314 KRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeKLEKEL 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  257 LQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEN--------------------------ELANKEAILRQMEE 310
Cdd:PRK03918   394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEE 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  311 KNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 383
Cdd:PRK03918   474 KERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  384 REKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESENFRK---NLEESLHDKERLAEEIEKLRSELD 460
Cdd:PRK03918   554 LKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELEREEKELKKLEEELD 629


                   .
gi 1327850359  461 Q 461
Cdd:PRK03918   630 K 630
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-461 4.12e-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: 70.86  E-value: 4.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  216 RLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC---YLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMND 292
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQKELYALANE---ISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  293 KLENELANKEAILRQMEEKNRQLQE----RLELAEQKLQQTMRKAETLPEVEAELAQriaaLTKAEERHGNIEERMRHLE 368
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELE 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  369 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESENFRKNLEESLHDKE 446
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELE 457

                          250
                   ....*....|....*
gi 1327850359  447 RLAEEIEKLRSELDQ 461
Cdd:TIGR02168  458 RLEEALEELREELEE 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
101-469 6.44e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.01  E-value: 6.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  101 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIVA-LREQNvhiqrkMVSSEGSTESEHLEGMEAGQKVHE 179
Cdd:PRK03918   162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKELEEvLREIN------EISSELPELREELEKLEKEVKELE 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  180 KRlsngsidstddTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRdIRECY 256
Cdd:PRK03918   235 EL-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIK-LSEFY 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  257 LQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLq 327
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL- 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  328 qtmrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTV 399
Cdd:PRK03918   382 ----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEY 457

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  400 DRLLTESNERLQ-LHLKERMAALEEKNV---LIQESENFR--------KNLEESL--HDKERL---AEEIEKLRSELDQM 462
Cdd:PRK03918   458 TAELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKL 537


                   ....*..
gi 1327850359  463 KMRTGSL 469
Cdd:PRK03918   538 KGEIKSL 544
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
27-465 8.03e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 8.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSL 106
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEE 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES-EHLEGMEAGQKVHEKRLSNG 185
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGL 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  186 SIDstddtsQIVELQELLEKQNYEMaqmKERLTALSSRVGEVEQEAETARKDLIKTE-----------EMNTKYQRDIRE 254
Cdd:PRK03918   385 TPE------KLEKELEELEKAKEEI---EEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLE 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  255 CYLqamAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAI--LRQMEEKNRQLQERLE-LAEQKLQQTMR 331
Cdd:PRK03918   456 EYT---AELKRIEKELKEIEEKERKLRKELR-------ELEKVLKKESELikLKELAEQLKELEEKLKkYNLEELEKKAE 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  332 KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERL 410
Cdd:PRK03918   526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYL 605

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  411 QLHLKERMAALEEKNVLIQESEnfrknLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:PRK03918   606 ELKDAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLEELRKELEELEKK 655
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 41-390 1.35e-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: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   41 EQLLEKEEEISElKAERNNTRL--LLEHLECLVSRHERSLRMTVVKRQAQSPSG--VSSEVEVLKALKSLFEHHKALDEK 116
Cdd:TIGR02169  173 EKALEELEEVEE-NIERLDLIIdeKRQQLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  117 VRERLRVSLE----RVSALEEELAAANQEIVAL-REQNVHIQRKMVSSEGSTESehlegMEAGQKVHEKRLSNGSIDSTD 191
Cdd:TIGR02169  252 ELEKLTEEISelekRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIAS-----LERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  192 DTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREcylqamaqKEDMEERIT 271
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDE--------LKDYREKLE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  272 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALT 351
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----------DKALEIKKQEWKLEQLAADLS 465

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1327850359  352 KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 390
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-459 1.64e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQAQspsgvssEVEVLKALK 104
Cdd:PRK03918   236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE------EKVKELKELKEKAE-------EYIKLSEFY 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  105 SLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTES-EHLEGMEAGQKVHEKRLS 183
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLT 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  184 NGSIDstddtsQIVELQELLEKQNYEmaqMKERLTALSSRVGEVEQEAETARKDLIKTE-------------------EM 244
Cdd:PRK03918   383 GLTPE------KLEKELEELEKAKEE---IEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteehrkEL 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  245 NTKYQR---DIRECYLQAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQE 317
Cdd:PRK03918   454 LEEYTAelkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKE 532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  318 RLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNk 393
Cdd:PRK03918   533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFYNEYL- 605

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  394 RLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKE--RLAEEIEKLRSEL 459
Cdd:PRK03918   606 ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeELREEYLELSREL 675
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-387 1.74e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 65.17  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVS 94
Cdd:COG4717     88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEE 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEgmeag 174
Cdd:COG4717    168 LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE----- 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  175 QKVHEKRLSN----------GSIDSTDDTSQIVE------------LQELLEKQNYEMAQMKERLTALSSRvgevEQEAE 232
Cdd:COG4717    243 ERLKEARLLLliaaallallGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPAL----EELEE 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  233 TARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKn 312
Cdd:COG4717    319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY- 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  313 RQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQR 384
Cdd:COG4717    398 QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQE 477


                   ...
gi 1327850359  385 EKM 387
Cdd:COG4717    478 LEE 480
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-463 6.13e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   41 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 118
Cdd:PRK03918   286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  119 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEagQKVHEKRLSNGSIDSTDDTSQIV 197
Cdd:PRK03918   364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  198 -------ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----RDIRECY-------LQ 258
Cdd:PRK03918   442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlKELEEKLkkynleeLE 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  259 AMAQK-EDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 330
Cdd:PRK03918   522 KKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  331 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 410
Cdd:PRK03918   602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  411 QLHLKERMAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 463
Cdd:PRK03918   675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-459 1.12e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 107
Cdd:PRK03918   315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  108 EHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMVSSEGSTESE 166
Cdd:PRK03918   395 ELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEE 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  167 HLEGMEAGQKVHEKRLSNGS--IDSTDDTSQIVELQELLEKQNYEMAQMKER-LTALSSRVGEVEQEAETARKDLIKTEE 243
Cdd:PRK03918   474 KERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEE 553

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  244 MNTKYQRDIREcylqamaqKEDMEERITTLEKRYLSAQREstSIHDMNDKLE---------NELANKEAILRQMEEKNRQ 314
Cdd:PRK03918   554 LKKKLAELEKK--------LDELEEELAELLKELEELGFE--SVEELEERLKelepfyneyLELKDAEKELEREEKELKK 623

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  315 LQERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHN 392
Cdd:PRK03918   624 LEEELDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EEL 685

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  393 KRLSDTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESENFRKNLEeslhDKERLAEEIEKLRSEL 459
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 ...
 34-462 2.22e-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: 61.91  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   34 KELNACREQLLEKEEEISELKAERNNtrlLLEHLECLVsrhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKAL 113
Cdd:TIGR00618  472 EQQLQTKEQIHLQETRKKAVVLARLL---ELQEEPCPL---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE 544

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  114 dEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstESEHLEGMEAGQKVHEKRLSNGSIDSTDDT 193
Cdd:TIGR00618  545 -EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC---------------DNRSKEDIPNLQNITVRLQDLTEKLSEAED 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTL 273
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQDLQDVRLH-------LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  274 EKRYLSAQRESTSIHDM----NDKLENELANKEAILRQMEE-------KNRQLQERLELAEQKLQQTMRKAET-LPEVEA 341
Cdd:TIGR00618  682 LQKMQSEKEQLTYWKEMlaqcQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTvLKARTE 761

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  342 ELAQRIAALTKAEERhgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL 421
Cdd:TIGR00618  762 AHFNNNEEVTAALQT----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1327850359  422 EEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 462
Cdd:TIGR00618  838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 261-469 3.02e-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: 61.62  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET----L 336
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  337 PEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqrEKMNEEHnKRLSDTVDRLLTESNERLQL--HL 414
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------SKLEEEV-SRIEARLREIEQKLNRLTLEkeYL 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  415 KERMAALEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 469
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 258-468 3.75e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.16  E-value: 3.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  258 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLp 337
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ- 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  338 evEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 399
Cdd:COG4942    103 --KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850359  400 DRLLTEsNERLQLHLKERMAALEEKNvliQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGS 468
Cdd:COG4942    181 AELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 827-893 4.03e-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: 4.03e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359   827 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 893
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 181-469 4.57e-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: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  181 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemntkyqRDIRECYLQAM 260
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLE 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLelAEQKLQQTMRKAETLPEVE 340
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEV 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  341 AELAQRIAALTKAEERhgnieermRHLEGQ-LEEKNQELQrarqrEKMNEEHNKRlsdtvdrlltESNERLQLHLKERMA 419
Cdd:TIGR02169  808 SRIEARLREIEQKLNR--------LTLEKEyLEKEIQELQ-----EQRIDLKEQI----------KSIEKEIENLNGKKE 864

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327850359  420 ALEEKnvlIQESENFRKNLEESLHDkerLAEEIEKLRSELDQMKMRTGSL 469
Cdd:TIGR02169  865 ELEEE---LEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
PTZ00121 PTZ00121
MAEBL; Provisional
 35-444 4.65e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 114
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVHEKRLSNgSIDSTDD 192
Cdd:PTZ00121  1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARkdlikTEEMNTKYQRdirECYLQAMAQKEDMEERITT 272
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-----IEEVMKLYEE---EKKMKAEEAKKAEEAKIKA 1622

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAEL 343
Cdd:PTZ00121  1623 EELK--KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEE 1700

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  344 AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAA 420
Cdd:PTZ00121  1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAV 1780

                          410       420
                   ....*....|....*....|....
gi 1327850359  421 LEEKnvLIQESENFRKNLEESLHD 444
Cdd:PTZ00121  1781 IEEE--LDEEDEKRRMEVDKKIKD 1802
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-462 4.76e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTV------VKRQAQSPSGVSSEVEVL 100
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleelAEELLEALRAAAELAAQL 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  101 KALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEK 180
Cdd:COG1196    403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  181 RLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG-----EVEQEAETARKDLIKTEEMNTKYQRDIREC 255
Cdd:COG1196    483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligvEAAYEAALEAALAAALQNIVVEDDEVAAAA 562

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  256 --YLQAMAQKEDMEERITTLEKRYLSAQ-RESTSIHDMNDKLENELANKEAILR--QMEEKNRQLQERLELAEQKLQQTM 330
Cdd:COG1196    563 ieYLKAAKAGRATFLPLDKIRARAALAAaLARGAIGAAVDLVASDLREADARYYvlGDTLLGRTLVAARLEAALRRAVTL 642

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  331 RKAETLPEVEAELAQRIAALTKAEERHGN-----IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE 405
Cdd:COG1196    643 AGRLREVTLEGEGGSAGGSLTGGSRRELLaalleAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  406 SNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 462
Cdd:COG1196    723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 33-456 4.84e-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: 60.83  E-value: 4.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   33 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPSGVSSEV-EVLKAL-KSLFEHH 110
Cdd:TIGR00606  411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIlELDQELrKAERELS 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  111 KALDEKVRERLrvsLERVSALEEELAAANQEIVALREQNVHIQRKmVSSEGSTESEHLEGMEAGQKVHE--KRLSNGSID 188
Cdd:TIGR00606  489 KAEKNSLTETL---KKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKikSRHSDELTS 564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  189 STDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqaMAQKEDMEE 268
Cdd:TIGR00606  565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEES 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  269 RITTLEKRYLSAQRESTSIH---DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELA 344
Cdd:TIGR00606  640 DLERLKEEIEKSSKQRAMLAgatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELK 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  345 ----QRIAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEHNKRLSDTV-------DRLLTESN--ERLQ 411
Cdd:TIGR00606  720 kkekRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTimERFQ 798

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  412 LHLKERMAALEEKNVLIQESE------NFRKNLEESLHDKERLAEEIEKLR 456
Cdd:TIGR00606  799 MELKDVERKIAQQAAKLQGSDldrtvqQVNQEKQEKQHELDTVVSKIELNR 849
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 194-390 5.12e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.84  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIrecylqaMAQKEDMEERITTL 273
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-------AEAEAEIEERREEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  274 EKRYLSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET 335
Cdd:COG3883     89 GERARALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEA 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  336 -LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 390
Cdd:COG3883    169 aKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-463 5.82e-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: 60.46  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  226 EVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA-MAQK-EDMEERITTLEKRYLSAQREStsihdmndkLENELANKEA 303
Cdd:TIGR02168  176 ETERKLERTRENLDRLEDILNELERQLKSLERQAeKAERyKELKAELRELELALLVLRLEE---------LREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  304 ILRQMEEKNRQLQERLELAEQKLQQTMRKaetlpevEAELAQRIAALTKAEERHGNIEERmrhLEGQLEEKNQELQRARQ 383
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISR---LEQQKQILRERLANLER 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  384 REKMNE---EHNKRLSDTVDRLLTESNERLQLhLKERMAALEEKnvlIQESENFRKNLEESLHDKErlaEEIEKLRSELD 460
Cdd:TIGR02168  317 QLEELEaqlEELESKLDELAEELAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVA 389


                   ...
gi 1327850359  461 QMK 463
Cdd:TIGR02168  390 QLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 191-615 6.58e-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: 60.47  E-value: 6.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  191 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecYLQAMAQKEDMEERI 270
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER------------YQALLKEKREYEGYE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  271 TTLEKRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAAL 350
Cdd:TIGR02169  228 LLKEKEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVK 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  351 TKAEERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKRLSdtvdrlltesnerlqlhlkermaaleeknvliq 429
Cdd:TIGR02169  294 EKIGELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDKLLA--------------------------------- 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  430 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLieptisrthidtSTELRYSVGSLVDSQSDYRTTKVIRRPR 509
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINEL 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  510 RGRMGVRRDEPKVKS--LGDHEwnrtQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQL 587
Cdd:TIGR02169  405 KRELDRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEY 478

                          410       420
                   ....*....|....*....|....*...
gi 1327850359  588 DAINKEIRLIQEEKESTELRAEEIENRV 615
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 52-390 9.30e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 9.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   52 ELKAERNntrlLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSA- 130
Cdd:COG1196    217 ELKEELK----ELEAELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAe 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  131 ---LEEELAAANQEIVALREQNVHIQRkmvssegstesehlegmeagqkvhekrlsngsidstddtsQIVELQELLEKQN 207
Cdd:COG1196    290 eyeLLAELARLEQDIARLEERRRELEE----------------------------------------RLEELEEELAELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  208 YEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEmntkyqrdirecylQAMAQKEDMEERITTLEKRYLSAQRESTSI 287
Cdd:COG1196    330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEE--------------ALLEAEAELAEAEEELEELAEELLEALRAA 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  288 HDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 367
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                          330       340
                   ....*....|....*....|...
gi 1327850359  368 EGQLEEKNQELQRARQREKMNEE 390
Cdd:COG1196    476 EAALAELLEELAEAAARLLLLLE 498
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 95-439 2.10e-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: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVR---------ERLRVS-------LERVSALEEELAAANQEIValREQNVHIQRKMVS 158
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQqekfekmeqERLRQEkeekareVERRRKLEEAEKARQAEMD--RQAAIYAEQERMA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  159 SEGSTESEHLegmeagqKVHEKRLSNGSIDSTDDTSQIVELQELlEKQNYEMAQMKERltalssrvgeVEQEAETARKDL 238
Cdd:pfam17380  344 MERERELERI-------RQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVK 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  239 IKTEEMNTKYQRDIRECYL----QAMAQKEDM----EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 310
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQiraeQEEARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  311 KNRQLQERLELAEQKLQQtmRKAETLPE------VEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEknqelqRARQR 384
Cdd:pfam17380  486 RKRAEEQRRKILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQE--MEE------RRRIQ 555

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  385 EKMneehnkrlsdtvdRLLTESNERLQLHLKERmaaleEKNVLIQESENFRKNLE 439
Cdd:pfam17380  556 EQM-------------RKATEERSRLEAMERER-----EMMRQIVESEKARAEYE 592
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-458 2.20e-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: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  292 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLE 368
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  369 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESENFRKNLEES 441
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778

                          170
                   ....*....|....*..
gi 1327850359  442 LHDKERLAEEIEKLRSE 458
Cdd:COG4913    779 RARLNRAEEELERAMRA 795
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 27-466 2.32e-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: 58.65  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHE-RSLRMTVVKRQAQSpsgvssevevlkALKS 105
Cdd:pfam01576   40 EEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEeRSQQLQNEKKKMQQ------------HIQD 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  106 LFEHhkaLDEKVRERLRVSLERVSaLEEELAAANQEIVALREQNVHIQRKM---------VSSEGSTESEHLEGMEAGQK 176
Cdd:pfam01576  108 LEEQ---LDEEEAARQKLQLEKVT-TEAKIKKLEEDILLLEDQNSKLSKERklleeriseFTSNLAEEEEKAKSLSKLKN 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  177 VHE-----------------------KRLSNGsiDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAET 233
Cdd:pfam01576  184 KHEamisdleerlkkeekgrqelekaKRKLEG--ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  234 ARKDLIKTEEMNTKYQRDI---RECYLQAMAQKEDMEERI------------TTLEKRYLSAQREsTSIHDMNDKLENEL 298
Cdd:pfam01576  262 ALKKIRELEAQISELQEDLeseRAARNKAEKQRRDLGEELealkteledtldTTAAQQELRSKRE-QEVTELKKALEEET 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  299 ANKEAILRQMEEKNRQ----LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEerhGNIEERMRHLEGQLEEK 374
Cdd:pfam01576  341 RSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK---QDSEHKRKKLEGQLQEL 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  375 NQELQRA-RQREKMNEEHNK--------------------RLSDTVDRL---LTESNERLQ------LHLKERMAALEEk 424
Cdd:pfam01576  418 QARLSESeRQRAELAEKLSKlqselesvssllneaegkniKLSKDVSSLesqLQDTQELLQeetrqkLNLSTRLRQLED- 496

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1327850359  425 nvliqESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRT 466
Cdd:pfam01576  497 -----ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL 533
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 112-460 2.48e-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: 58.81  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQ------RKMVSSEGSTESEHLEgmeagQKVHEKRlsng 185
Cdd:COG3096    829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllNKLLPQANLLADETLA-----DRLEELR---- 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  186 sidstddtsqiVELQELLEKQNYeMAQMKERLTalssrvgEVEQEAETARKDLIKTEEMntkyQRDirecYLQAMAQKED 265
Cdd:COG3096    900 -----------EELDAAQEAQAF-IQQHGKALA-------QLEPLVAVLQSDPEQFEQL----QAD----YLQAKEQQRR 952

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  266 MEERITTLEkrYLSAQRESTSIHD----------MNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET 335
Cdd:COG3096    953 LKQQIFALS--EVVQRRPHFSYEDavgllgensdLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA 1030

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  336 LPEVEAELAQRIAAL-----TKAEERhgnIEERMRHLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTE 405
Cdd:COG3096   1031 KQQTLQELEQELEELgvqadAEAEER---ARIRRDELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQ 1105

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  406 SNERLQLHLKERMAALEeknvLIQESenfrkNLEESLHDKERLAEEIEKLRSELD 460
Cdd:COG3096   1106 EREQVVQAKAGWCAVLR----LARDN-----DVERRLHRRELAYLSADELRSMSD 1151
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 194-460 2.78e-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: 57.38  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyqRDIRECYLQAMAQKEDMEER---I 270
Cdd:pfam19220   48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE-------AALREAEAAKEELRIELRDKtaqA 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  271 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 350
Cdd:pfam19220  121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  351 TKAEERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNerlqlhlkeRMAALEeknVLIQ 429
Cdd:pfam19220  201 ETQLDAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASLRMKLEALTA---------RAAATE---QLLA 265

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1327850359  430 ESENFRKNLEESLHDKERLAEEIEKLRSELD 460
Cdd:pfam19220  266 EARNQLRDRDEAIRAAERRLKEASIERDTLE 296
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-381 3.10e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLeclvsrheRSLRMTVVKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEA--------QAEEYELLAELARLEQDIARLEERRRELEER 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEhlegmEAGQKVHEKRLSNGS 186
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-----EEELEELAEELLEAL 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNtkyqrdirecyLQAMAQKEDM 266
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-----------AELEEEEEAL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVEAELAQR 346
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAA 539

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1327850359  347 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 381
Cdd:COG1196    540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 41-482 3.39e-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: 58.13  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   41 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 115
Cdd:TIGR00606  684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  116 KVrERLRVSLERVSAL------EEELAAANQEIVALREQnVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS 189
Cdd:TIGR00606  759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  190 TDDT--SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTkyqrDIRECYLQAMAQKEDME 267
Cdd:TIGR00606  837 ELDTvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST----EVQSLIREIKDAKEQDS 912

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  268 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 347
Cdd:TIGR00606  913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  348 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 424
Cdd:TIGR00606  984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  425 NVLIQESENF-----RKNLEESLHDKERLAEEI-----EKLRSELDQMKMRTGSLIEPTISRTHIDTS 482
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQA 1130
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-357 3.68e-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: 3.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALK 104
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEI 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  105 SLFEHHKaldekvrERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMVSSEgstesehlegmeagqkvhekrlsn 184
Cdd:TIGR02168  298 SRLEQQK-------QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE------------------------ 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  185 gsidstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKE 264
Cdd:TIGR02168  344 ---------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE----RLEARLE 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  265 DMEERITTLEKRyLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 344
Cdd:TIGR02168  411 RLEDRRERLQQE-IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                          330
                   ....*....|...
gi 1327850359  345 QRIAALTKAEERH 357
Cdd:TIGR02168  489 ARLDSLERLQENL 501
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 32-470 4.10e-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: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 111
Cdd:TIGR04523  171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  112 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMV--SSEGSTESEHLEGMEAGQKVHEKRLSNGSIDS 189
Cdd:TIGR04523  233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  190 TDDTSQivELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylqamaqKEDMEER 269
Cdd:TIGR04523  305 EQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE--------KQNEIEK 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  270 IttlekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 349
Cdd:TIGR04523  375 L----------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  350 LTKA----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlq 411
Cdd:TIGR04523  445 LTNQdsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS--- 521

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  412 lhLKERMAALE----EKNVLIQESENFRKNLEESLhDKERLAEEIEKLRSELDQMKMRTGSLI 470
Cdd:TIGR04523  522 --LKEKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
PRK01156 PRK01156
chromosome segregation protein; Provisional
 35-411 5.24e-08

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 57.22  E-value: 5.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   35 ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 114
Cdd:PRK01156   333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKIQEIDPDAIK 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 eKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNGSIDSTDDTS 194
Cdd:PRK01156   409 -KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRLEE 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNYEMAQMKERLTALSSrvGEVEQ------EAETARKDLIKTE-------EMNTKYQ------------ 249
Cdd:PRK01156   484 KIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLEDIKikinelkDKHDKYEeiknrykslkle 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  250 --RDIRECYLQAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDKLENELANKEA----ILRQMEEKNRQLQERLELAE 323
Cdd:PRK01156   562 dlDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQ 639

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  324 QK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVd 400
Cdd:PRK01156   640 ENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI- 718

                          410
                   ....*....|.
gi 1327850359  401 rllTESNERLQ 411
Cdd:PRK01156   719 ---NDINETLE 726
PTZ00121 PTZ00121
MAEBL; Provisional
 45-474 6.91e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   45 EKEEEISELKAERNNTRLllehlECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRErlrvs 124
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKA-----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK----- 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  125 lervsalEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHL-EGMEAGQKVHEKRLSNGSIDSTDDTSQIVE---LQ 200
Cdd:PTZ00121  1433 -------ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEAKKKAEEAKKKADeakKA 1505

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  201 ELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK--DLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYL 278
Cdd:PTZ00121  1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  279 SAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 349
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  350 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEknvLIQ 429
Cdd:PTZ00121  1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE---AKK 1737

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1327850359  430 ESENFRKNLEESLHDKERlAEEIEKLRSELDQMKMRTGSLIEPTI 474
Cdd:PTZ00121  1738 EAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVI 1781
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 118-457 8.52e-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: 56.88  E-value: 8.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  118 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQR---KMVSSEGSTE------SEHLEGMEAGQKVHEKrlsngsID 188
Cdd:COG3096    277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAReleELSARESDLEqdyqaaSDHLNLVQTALRQQEK------IE 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  189 STDDtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE------CYLQAMAQ 262
Cdd:COG3096    351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVqqtraiQYQQAVQA 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 KEDMEERittLEKRYLSAqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PE 338
Cdd:COG3096    422 LEKARAL---CGLPDLTP-----------ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGE 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  339 VEAELA-QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKER 417
Cdd:COG3096    488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAEL 562

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1327850359  418 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRS 457
Cdd:COG3096    563 EAQLEE---LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 959-1014 9.05e-08

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: 9.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359   959 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 195-409 9.37e-08

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: 55.54  E-value: 9.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLe 274
Cdd:COG4942     35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  275 krYLSAQRESTSI----HDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 350
Cdd:COG4942    114 --YRLGRQPPLALllspEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850359  351 TKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 409
Cdd:COG4942    191 EALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
280-460 1.70e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  280 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 359
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  360 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLKERmaaLEEKNVLIQESENFRKNLE 439
Cdd:PRK02224   277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-----LRDR---LEECRVAAQAHNEEAESLR 348

                          170       180
                   ....*....|....*....|.
gi 1327850359  440 ESLHDKERLAEEIEKLRSELD 460
Cdd:PRK02224   349 EDADDLEERAEELREEAAELE 369
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-465 1.93e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 352
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  353 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 429
Cdd:COG4717    131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1327850359  430 ESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:COG4717    200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-401 2.15e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSL 106
Cdd:COG1196    456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHH--KALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrKMVSSEGSTESEHLEGMEAGQKVHEKRLSN 184
Cdd:COG1196    536 YEAAleAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD-----KIRARAALAAALARGAIGAAVDLVASDLRE 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  185 GSIDSTDDTSQIVELQELLEKqnyeMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKE 264
Cdd:COG1196    611 ADARYYVLGDTLLGRTLVAAR----LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  265 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 344
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  345 QRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 401
Cdd:COG1196    767 RELERLEREIEALGPVnllaieeyeelEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 191-459 3.14e-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: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  191 DDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVE-QEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 269
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  270 ITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAETLPEVEAELAQRI 347
Cdd:pfam02463  239 IDLLQELLRDEQEEIES---SKQEIEKEEEKLAQVLKENKEEEKekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  348 AA-----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 419
Cdd:pfam02463  316 LKesekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1327850359  420 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSEL 459
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 119-471 4.84e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.20  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  119 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstESEHLEGMEAGQKVHEKRLSNgsidstddtsQIVE 198
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE---EQLKKQQLLKQLRARIEELRA----------QEAV 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  199 LQELLEKQNYemAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdIRECYLQAMAQKEDMEERITTLEkryl 278
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK----LLMKRAAHVKQQSSIEEQRRLLQ---- 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  279 SAQRESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTK 352
Cdd:TIGR00618  349 TLHSQEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQ 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  353 AEERHGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------ 413
Cdd:TIGR00618  426 LAHAKKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcp 505

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  414 LKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 471
Cdd:TIGR00618  506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 305-463 4.91e-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: 53.61  E-value: 4.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  305 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQR 384
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  385 EKMNEEHNKRLSDTVDRL--------------LTESNERLQLH---LKERMAALEEKNVLIQESENFRKNLEESLHDKER 447
Cdd:COG4942     99 LEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERAELEA 178

                          170
                   ....*....|....*.
gi 1327850359  448 LAEEIEKLRSELDQMK 463
Cdd:COG4942    179 LLAELEEERAALEALK 194
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1037-1108 5.28e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 5.28e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  1037 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1108
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 31-464 5.77e-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: 54.03  E-value: 5.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   31 ALTKELNACREQLLEKEEEISELKAERNNTRlllEHLECLVSR--HERSLRMTVVKRQAQSPSGVSSevevlkaLKSLFE 108
Cdd:pfam01576  212 KLEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARleEETAQKNNALKKIRELEAQISE-------LQEDLE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  109 HHKALDEKVRERLRVSLERVSALEEEL------AAANQEIVALREQNVHIQRKMVSSEGstesehlegmeagqKVHEKRL 182
Cdd:pfam01576  282 SERAARNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVTELKKALEEET--------------RSHEAQL 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  183 SNGSIDSTddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETarkdlIKTEEMNTKYQRDIRECYLQamaq 262
Cdd:pfam01576  348 QEMRQKHT---QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRT-----LQQAKQDSEHKRKKLEGQLQ---- 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 kedmeeritTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaETLPEveaE 342
Cdd:pfam01576  416 ---------ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ---ELLQE---E 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  343 LAQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEEHNKRLSDTVDRLLTESnerlqlhlkERMAALE 422
Cdd:pfam01576  481 TRQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDA---------GTLEALE 544

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1327850359  423 E-KNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKM 464
Cdd:pfam01576  545 EgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-352 6.11e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 6.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspsgvSSEVEVLKALKSL 106
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDL---------------HKLEEALNDLEAR 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKAldEKVRERLRVSLERVSALEEELAAANQEIvalreQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGS 186
Cdd:TIGR02169  788 LSHSRI--PEIQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IdstddtsQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRdIRECYLQAMAQKEDM 266
Cdd:TIGR02169  861 G-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEK-KRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQR 346
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008


                   ....*.
gi 1327850359  347 IAALTK 352
Cdd:TIGR02169 1009 IEEYEK 1014
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 29-387 6.26e-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: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   29 FAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHER---SLRMTVVKRQAQSPS---GVSSEVEVLKA 102
Cdd:pfam19220   57 LAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAakeELRIELRDKTAQAEAlerQLAAETEQNRA 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKslfEHHKALdekvRERLRVSLERVSALEEELAAAnQEIVALREQNVHIQRKMVSSEGSTESEHlegmEAGQKVHEKRL 182
Cdd:pfam19220  137 LE---EENKAL----REEAQAAEKALQRAEGELATA-RERLALLEQENRRLQALSEEQAAELAEL----TRRLAELETQL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  183 SNGSIDSTDDTSQIVELQELLEK----QNYEMAQMKERLTALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirecylQ 258
Cdd:pfam19220  205 DATRARLRALEGQLAAEQAERERaeaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-----------E 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  259 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpe 338
Cdd:pfam19220  267 ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA----- 333

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  339 veaeLAQRIAALTKAEERHGNIEERMRHLEGQ-------LEEKNQELQRARQREKM 387
Cdd:pfam19220  334 ----LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQANRRLKEELQRERA 385
mukB PRK04863
chromosome partition protein MukB;
118-455 7.04e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.81  E-value: 7.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  118 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRK---MVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDts 194
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDL-------IKTEEMNTKYQ------RDIREC------ 255
Cdd:PRK04863   356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqalDVQQTRAIQYQqavqalERAKQLcglpdl 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  256 -------YL-QAMAQKEDMEERITTLEKRyLSAQRESTSIHD--------MNDKLENELANKEAI--------------- 304
Cdd:PRK04863   436 tadnaedWLeEFQAKEQEATEELLSLEQK-LSVAQAAHSQFEqayqlvrkIAGEVSRSEAWDVARellrrlreqrhlaeq 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  305 ----------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 374
Cdd:PRK04863   515 lqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  375 NQELQRARQrekmnEEHNkrLSDTVDRLLTESNERLqlhlkERMAALEE--KNVLIQESEnFRKNLEESLHDKERLAEEI 452
Cdd:PRK04863   595 IQRLAARAP-----AWLA--AQDALARLREQSGEEF-----EDSQDVTEymQQLLERERE-LTVERDELAARKQALDEEI 661


                   ...
gi 1327850359  453 EKL 455
Cdd:PRK04863   662 ERL 664
PRK12704 PRK12704
phosphodiesterase; Provisional
 297-454 8.83e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 8.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  297 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 376
Cdd:PRK12704    34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  377 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 453
Cdd:PRK12704   111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179


                   .
gi 1327850359  454 K 454
Cdd:PRK12704   180 E 180
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 25-422 8.88e-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: 53.58  E-value: 8.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   25 TFQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPSGVSSEVEVLKALK 104
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRSRVDLKLQELQHLK 537

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  105 SLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMVSSEGSTESE-HLEGMEAGQKVHEKRLS 183
Cdd:pfam15921  538 NEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQ-IENMTQLVGQHGRTAGAmQVEKAQLEKEINDRRLE 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  184 NGSIDSTDDT--SQIVELQELLEKQNYEMAQM----KERLTALSSRVGEVEQ---EAETARKDLIKTEEMNTKYQRDIRE 254
Cdd:pfam15921  606 LQEFKILKDKkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRN 685

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  255 cylqamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQKLQ 327
Cdd:pfam15921  686 -------KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMT 758

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  328 QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLTESN 407
Cdd:pfam15921  759 NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQ 832

                          410
                   ....*....|....*
gi 1327850359  408 ERLQLHLKERMAALE 422
Cdd:pfam15921  833 ESVRLKLQHTLDVKE 847
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 257-462 1.09e-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: 53.05  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  257 LQAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK------L 326
Cdd:TIGR00618  183 LMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  327 QQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDRLL 403
Cdd:TIGR00618  263 KQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKRAAHVKQQSSIEE 342

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  404 TESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLH----DKERLAEEIEKLRSELDQM 462
Cdd:TIGR00618  343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDIL 405
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
70-365 1.32e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   70 LVSRHERSLRMTVVKRQAQSPSGVSSEVEVLK-------ALKSL---------FEHHKALDEKVRERLRVSLERVSAL-- 131
Cdd:COG3206     60 LVEPQSSDVLLSGLSSLSASDSPLETQIEILKsrpvlerVVDKLnldedplgeEASREAAIERLRKNLTVEPVKGSNVie 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  132 ------EEELAA--ANQEIVALREQNvhIQRKMVSSEGSTE--SEHLEGM-----EAGQKVHEKRLSNGSIDSTDDT--- 193
Cdd:COG3206    140 isytspDPELAAavANALAEAYLEQN--LELRREEARKALEflEEQLPELrkeleEAEAALEEFRQKNGLVDLSEEAkll 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 -SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAetarkdlikTEEMNTKYQRDIRECYLQAMAQKEDMEERITT 272
Cdd:COG3206    218 lQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL---------PELLQSPVIQQLRAQLAELEAELAELSARYTP 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQREstsIHDMNDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 352
Cdd:COG3206    289 NHPDVIALRAQ---IAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362

                          330
                   ....*....|...
gi 1327850359  353 AEERHGNIEERMR 365
Cdd:COG3206    363 ARELYESLLQRLE 375
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 27-534 1.55e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.53  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSS 95
Cdd:pfam12128  279 EERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQS 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   96 EVEVL-KALKSLFEHHKALDEKV-RERLRVSLE---RVSALEEELAAANQEIVALREqnvhiqrkmvssegsTESEHLEG 170
Cdd:pfam12128  355 ELENLeERLKALTGKHQDVTAKYnRRRSKIKEQnnrDIAGIKDKLAKIREARDRQLA---------------VAEDDLQA 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  171 MEAG-QKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmAQMKERLTALSSRVGEV--EQEAETARKDLIKTEEMNTK 247
Cdd:pfam12128  420 LESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAreEQEAANAEVERLQSELRQAR 498

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  248 YQRDIRECYLQAMAQKedMEERITTLEKRYLSAQRESTSIH-----DMNDKLEN--ELANKEAILR---QMEEKNRQLQE 317
Cdd:pfam12128  499 KRRDQASEALRQASRR--LEERQSALDELELQLFPQAGTLLhflrkEAPDWEQSigKVISPELLHRtdlDPEVWDGSVGG 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  318 RLELAEQKLQ----QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 393
Cdd:pfam12128  577 ELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  394 RLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESENF-----RKNLEESLHDKERLAEEIEKLRSELDQMKm 464
Cdd:pfam12128  657 RLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK- 735

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  465 rTGSLIEPTISRTHIDT-STELRYSVGSL-VDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLgdHEWNRTQ 534
Cdd:pfam12128  736 -AAIAARRSGAKAELKAlETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQET 804
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 50-469 1.59e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.81  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   50 ISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL---RVSLE 126
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLE 492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  127 R----VSAL-------EEELAAANQEIVALREQ-NVHIQRkmvSSEGSTESEHLEGMEAGQKVHEKRLSngsidstdDTS 194
Cdd:pfam15921  493 SsertVSDLtaslqekERAIEATNAEITKLRSRvDLKLQE---LQHLKNEGDHLRNVQTECEALKLQMA--------EKD 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVE-LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcyLQAMAQKEDMEE-RITT 272
Cdd:pfam15921  562 KVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKvKLVN 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAALT 351
Cdd:pfam15921  640 AGSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLK 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  352 KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQEs 431
Cdd:pfam15921  717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQE- 777

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1327850359  432 enfrknLEESLHDKERLAEEIEKLRSELDQMKMRTGSL 469
Cdd:pfam15921  778 ------LSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 116-463 1.60e-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: 52.16  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  116 KVRERLRVSLERVSALEEELAAANQEIVALREQNvHIQRKMVssegstesEHLEGM--EAGQKVHEKRLSNG-SIDSTDD 192
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE-EKNREEV--------EELKDKyrELRKTLLANRFSYGpAIDELEK 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 T-----SQIVELQELLEKQNYEMA-----QMKERLTALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIRECYLQAMAQ 262
Cdd:pfam06160  154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYREMEEE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 KEDMEErittlekryLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAE 342
Cdd:pfam06160  227 GYALEH---------LNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAK 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  343 LaqriaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH-- 413
Cdd:pfam06160  287 K--------YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKev 357

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  414 ----LKERMAALEEKNVLIQES-ENFRKNLeESLHDKERLA-EEIEKLRSELDQMK 463
Cdd:pfam06160  358 ayseLQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 195-465 1.89e-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: 51.46  E-value: 1.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNYEMAQMKERLTALssrvgeVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLE 274
Cdd:pfam13868   81 QIEEREQKRQEEYEEKLQEREQMDEI------VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  275 KRYLSAQREstsihdMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 354
Cdd:pfam13868  155 ERILEYLKE------KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  355 ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEknvLIQESE-N 433
Cdd:pfam13868  229 KKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK---QIEEREeQ 305

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1327850359  434 FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:pfam13868  306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 32-454 2.36e-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: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   32 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 111
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQ--NVHIQRKMVSSEGSTESEHLEgmeagQKVHEKRLSNGSIDS 189
Cdd:TIGR04523  307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisQLKKELTNSESENSEKQRELE-----EKQNEIEKLKKENQS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  190 TDD-----TSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEE-----MNTKYQRDIRecYLQA 259
Cdd:TIGR04523  382 YKQeiknlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdlTNQDSVKELI--IKNL 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  260 MAQKEDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpev 339
Cdd:TIGR04523  460 DNTRESLETQLKVLSRSINKIKQNL-------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL--- 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  340 EAELAQriaaltkaeerhgnIEERMRHLEGQLEEKNQELQRArQREKMNEEHNKRLsdtvdrlltesnERLQLHLKERMA 419
Cdd:TIGR04523  530 ESEKKE--------------KESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEI------------EELKQTQKSLKK 582

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1327850359  420 ALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 454
Cdd:TIGR04523  583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 258-432 2.51e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  258 QAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAilrQMEEKNRQLQERLELAEQKLQQTMRKAETLP 337
Cdd:COG3883     27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREELGERARALYRSGGSVS 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  338 EVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 409
Cdd:COG3883    104 YLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                          170       180
                   ....*....|....*....|...
gi 1327850359  410 LQLHLKERMAALEEKNVLIQESE 432
Cdd:COG3883    184 LAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-465 2.64e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  118 RERLRVSLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehLEGMEAGQKVHEK--RLSNGSIDSTDDTSQ 195
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAE-------------------LDALQERREALQRlaEYSWDEIDVASAERE 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  196 IVELQ---ELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITT 272
Cdd:COG4913    670 IAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD----ELQDRLEAAEDLARL 745

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALT 351
Cdd:COG4913    746 ELRALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLP 815

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  352 KAEERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHL 414
Cdd:COG4913    816 EYLALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEA 888

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1327850359  415 KERM--AALEEKNVLIQESEN-FRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:COG4913    889 RPRPdpEVREFRQELRAVTSGaSLFDEELSEARFAALKRLIERLRSEEEESDRR 942
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 100-625 3.08e-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: 51.66  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  100 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEhlegMEAGQKVHE 179
Cdd:pfam15921   87 VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE----LEAAKCLKE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  180 KRLSNGSidstddtSQIVELQELLEKQNYEMAQMKERLTALSsrvgeveqeaETARKDLIKTEEMNTKYQRDIRECyLQA 259
Cdd:pfam15921  163 DMLEDSN-------TQIEQLRKMMLSHEGVLQEIRSILVDFE----------EASGKKIYEHDSMSTMHFRSLGSA-ISK 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  260 MAQKEDME-----ERITTLEKRYLSAQRESTS-----IHDMNDKLENELANKEAILRQMEEKN-------RQLQERLEL- 321
Cdd:pfam15921  225 ILRELDTEisylkGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAssarsqaNSIQSQLEIi 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  322 AEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDR 401
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  402 LLT-------------ESNERL-------QLHLKERMAALEEKNVLIQESENFRKNLEE-----------SLHDKERLAE 450
Cdd:pfam15921  382 LLAdlhkrekelslekEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaAIQGKNESLE 461

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  451 EIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELRYS--VGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPK-VKSLGD 527
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGD 541

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  528 HEWNRTQQIGVLGSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLAMMLQEQLDAINKEIRLIQEEKESTE 605
Cdd:pfam15921  542 HLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEKAQLEKEINDRRLELQEFKILKDKKD 617

                          570       580
                   ....*....|....*....|
gi 1327850359  606 LRAEEIENRVASVSLEGLNL 625
Cdd:pfam15921  618 AKIRELEARVSDLELEKVKL 637
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 195-373 3.31e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAmaqkEDMEERITTLE 274
Cdd:COG1579      8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  275 KR---------YLSAQRESTSIHDMNDKLEnelankEAILRQMEEKNrQLQERLELAEQKLQQtmrKAETLPEVEAELAQ 345
Cdd:COG1579     80 EQlgnvrnnkeYEALQKEIESLKRRISDLE------DEILELMERIE-ELEEELAELEAELAE---LEAELEEKKAELDE 149

                          170       180
                   ....*....|....*....|....*...
gi 1327850359  346 RIAALTKAEERhgnIEERMRHLEGQLEE 373
Cdd:COG1579    150 ELAELEAELEE---LEAEREELAAKIPP 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
194-477 3.80e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDMEERITTL 273
Cdd:COG4372     45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE----SLQEEAEELQEELEEL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  274 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKA 353
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKE 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  354 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEN 433
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1327850359  434 FRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIEPTISRT 477
Cdd:COG4372    272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 27-463 4.53e-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: 51.12  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAqSPSGVSSEVEVLKALKSL 106
Cdd:TIGR00618  386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA-ITCTAQCEKLEKIHLQES 464

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKV--RERLRVSLERVSALEEELAAANQEI-VALREQNVHIQRKMVSS-EGSTESEHLEGMEAGQKVHEKRL 182
Cdd:TIGR00618  465 AQSLKEREQQLqtKEQIHLQETRKKAVVLARLLELQEEpCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSE 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  183 SNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQ 262
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQ-KLQQTMRKAETLPEVEa 341
Cdd:TIGR00618  625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQsEKEQLTYWKEMLAQCQ- 703

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  342 ELAQRIAALTKAEERHGNIEERMRH-----LEGQLEEKNQELQRARqrekmneehnkRLSDTVDRLLTESNERLQLHLKE 416
Cdd:TIGR00618  704 TLLRELETHIEEYDREFNEIENASSslgsdLAAREDALNQSLKELM-----------HQARTVLKARTEAHFNNNEEVTA 772

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1327850359  417 RMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 463
Cdd:TIGR00618  773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 959-1010 6.07e-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: 44.54  E-value: 6.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  959 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1010
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 45-424 6.11e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.49  E-value: 6.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   45 EKEEEISELKAERNNTRLLLEHLECLVSRHERSLR------------MTVVKRQAQSPSgvsSEVEVLKALKS-----LF 107
Cdd:pfam05483  332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRteqqrleknedqLKIITMELQKKS---SELEEMTKFKNnkeveLE 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  108 EHHKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEK-RLS 183
Cdd:pfam05483  409 ELKKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeKLK 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  184 NGSI----------------DSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-KTEEMNT 246
Cdd:pfam05483  487 NIELtahcdklllenkeltqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqKGDEVKC 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  247 KY------QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELA 299
Cdd:pfam05483  567 KLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELA 646

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  300 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRH 366
Cdd:pfam05483  647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSE 726

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  367 LeGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLL---TESNERLQLHLKERMAALEEK 424
Cdd:pfam05483  727 L-GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEKLKMEAKENTAILKDK 786
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
26-435 6.79e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   26 FQEFAALTKELNACR---EQLLEKEEEISELKAErnntrllLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKA 102
Cdd:COG4717    131 YQELEALEAELAELPerlEELEERLEELRELEEE-------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQN-------VHIQRKMVSSEGSTESEHLEGMEAGQ 175
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaaLLALLGLGGSLLSLILTIAGVLFLVL 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  176 KVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREc 255
Cdd:COG4717    284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE- 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  256 ylqamAQKEDMEERITTLEKRYLsaqreSTSIHDMNDKLEnELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA-- 333
Cdd:COG4717    363 -----LQLEELEQEIAALLAEAG-----VEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEEle 431

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  334 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLE--GQLEEKNQELQRARQREKMNEEHNKRL---SDTVDRLLTESNE 408
Cdd:COG4717    432 EELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALklaLELLEEAREEYRE 511

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1327850359  409 RLQLHLKERMAAL-------EEKNVLIQESENFR 435
Cdd:COG4717    512 ERLPPVLERASEYfsrltdgRYRLIRIDEDLSLK 545
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-463 7.85e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQaqspsgvssevevlkaLKSL 106
Cdd:COG4717     81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE----------------LAEL 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVsLERVSALEEELAAANQEIVALREQnvhiqrkmvssegstesehlegmeagqkvhekrlsngs 186
Cdd:COG4717    145 PERLEELEERLEELREL-EEELEELEAELAELQEELEELLEQ-------------------------------------- 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 iDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDM 266
Cdd:COG4717    186 -LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGL 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA----E 342
Cdd:COG4717    265 GGSLLSLILTIAGVLFLVLGLLAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeellE 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  343 LAQRIAALTKAEERHGNIEERMRhLEGQLEEKNQELQRA--------RQREKMNEEHNKRLsdtvdRLLTESNERLQLHL 414
Cdd:COG4717    342 LLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAgvedeeelRAALEQAEEYQELK-----EELEELEEQLEELL 415

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1327850359  415 KERMAALE--EKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 463
Cdd:COG4717    416 GELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
264-465 8.56e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 8.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  264 EDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 337
Cdd:COG4913    245 EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARLEAELERLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  338 EVEAELAQRIAALTKAEERHGNIEErmrhleGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKER 417
Cdd:COG4913    316 ARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1327850359  418 MAALEEknvLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:COG4913    390 AALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 308-461 8.74e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 8.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  308 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 383
Cdd:COG1579      2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  384 R--------------------EKMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKnvLIQESENFRKNLEESLH 443
Cdd:COG1579     81 QlgnvrnnkeyealqkeieslKRRISDLEDEILELMERI--EELEEELAELEAELAELEAE--LEEKKAELDEELAELEA 156

                          170
                   ....*....|....*...
gi 1327850359  444 DKERLAEEIEKLRSELDQ 461
Cdd:COG1579    157 ELEELEAEREELAAKIPP 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 267-423 8.99e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 8.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  267 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqKLQQTMRKAETLPEVEAeLAQR 346
Cdd:COG1579     23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEA-LQKE 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  347 IAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 423
Cdd:COG1579     98 IESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-383 9.55e-06

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: 9.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEemntkyQRDIRECYLQAMAQKEDMEERITTLE 274
Cdd:COG4913    250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALR 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  275 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AA 349
Cdd:COG4913    323 EELDELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaAL 392

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1327850359  350 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 383
Cdd:COG4913    393 LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
193-486 1.07e-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: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 TSQIVELQELLEKQNYEMAQMKERLTALS--SRVGEVEQEAETARKDLIKTEEMntkyqrdiRECYLQAMAQKEDMEERI 270
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE--------LERLDASSDDLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  271 TTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAAL 350
Cdd:COG4913    695 EELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA 758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  351 tKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAALEE 423
Cdd:COG4913    759 -LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPEYEE 834

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  424 K--NVLIQESENFRKNLEESLHDKERLAEE-IEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELR 486
Cdd:COG4913    835 RfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 124-332 1.18e-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: 47.20  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  124 SLERVSALEEELAAANQEIVALREQNVHIQRKmvssegstesehlegmeagQKVHEKRLSNgsIDSTDDtsqivELQELL 203
Cdd:pfam15619    9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  204 EKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcylQAMAQKEDMEERITTLEKRYLSAQRE 283
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSED---KNLAEREELQKKLEQLEAKLEDKDEK 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  284 stsIHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 332
Cdd:pfam15619  140 ---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 295-461 2.03e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  295 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 374
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  375 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesenfRKNLEESLHDKER 447
Cdd:COG3883     92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161

                          170
                   ....*....|....
gi 1327850359  448 LAEEIEKLRSELDQ 461
Cdd:COG3883    162 LKAELEAAKAELEA 175
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-471 2.06e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   99 VLKALKSLFEhhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKmvSSEGSTESEHLEGMEAGQKVH 178
Cdd:COG4717     39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEEL 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  179 EKRLsngsidstDDTSQIVELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQ 258
Cdd:COG4717    115 REEL--------EKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  259 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQ----------- 327
Cdd:COG4717    183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallall 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  328 ----------------------------QTMRKAETLPEVEAELAQRIAALTKAEE--------RHGNIEERMRHLEGQL 371
Cdd:COG4717    263 glggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEeeleellaALGLPPDLSPEELLEL 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  372 EEKNQELQRA-RQREKMNEEHN-KRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQESENFRKNLEESL 442
Cdd:COG4717    343 LDRIEELQELlREAEELEEELQlEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1327850359  443 --HDKERLAEEIEKLRSELDQMKMRTGSLIE 471
Cdd:COG4717    423 eaLDEEELEEELEELEEELEELEEELEELRE 453
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 291-395 2.30e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  291 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGNIEERMR 365
Cdd:PRK00409   515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADEIIKELR 594

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1327850359  366 HLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 395
Cdd:PRK00409   595 QLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-313 2.31e-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: 48.91  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   28 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSL 106
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVR---ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKV--HEKR 181
Cdd:TIGR02169  314 ERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  182 LSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDlIKTEEMNTKYQRDIRECYLQama 261
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQ--- 469

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  262 QKEDMEERITTLEKRYLSAQREstsihdmndkleneLANKEAILRQMEEKNR 313
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRE--------------LAEAEAQARASEERVR 507
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
294-471 2.59e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  294 LENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 373
Cdd:PRK03918   174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  374 KNQELQRARQREKMNEEHNKRLSDtvdrlLTESNERLQlHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIE 453
Cdd:PRK03918   254 KRKLEEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327

                          170
                   ....*....|....*...
gi 1327850359  454 KLRSELDQMKMRTGSLIE 471
Cdd:PRK03918   328 ERIKELEEKEERLEELKK 345
PTZ00121 PTZ00121
MAEBL; Provisional
 107-454 3.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSteseHLEGMEAGQKVHEKRLSNgS 186
Cdd:PTZ00121  1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA----HFARRQAAIKAEEARKAD-E 1282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 IDSTDDTSQIVELQELLEKQNYE----MAQMKERLTALSSRVGEVEQEAETARKdliKTEEmnTKYQRDIRECYLQAMAQ 262
Cdd:PTZ00121  1283 LKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKK---KAEE--AKKAAEAAKAEAEAAAD 1357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 K-EDMEERITTLEKRYLSAQREStsihDMNDKLENELANKEAILRQMEEKNRQLQE--RLELAEQKLQQTMRKAETLPEV 339
Cdd:PTZ00121  1358 EaEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKA 1433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  340 EaELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESNERLQlhlkERMA 419
Cdd:PTZ00121  1434 D-EAKKKAEEAKKADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKAD----EAKK 1504

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1327850359  420 ALEEKnvliQESENFRKNLEESLHDKERLAEEIEK 454
Cdd:PTZ00121  1505 AAEAK----KKADEAKKAEEAKKADEAKKAEEAKK 1535
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 112-459 3.79e-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: 48.30  E-value: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  112 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLE-GMEAGQKVHEKRLSNGSIDST 190
Cdd:pfam12128  597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKALAER 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  191 DDTSQI------VELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDIRecylqama 261
Cdd:pfam12128  677 KDSANErlnsleAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAKAE-------- 748

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  262 QKEDMEERITTLEKRYLSAQRE---STSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LP 337
Cdd:pfam12128  749 LKALETWYKRDLASLGVDPDVIaklKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaIS 824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  338 EVEAELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKE 416
Cdd:pfam12128  825 ELQQQLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGE 890

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1327850359  417 RMAALEE-KNVLIQESENFRKNLEE-----SLHDKERLAEEIEKLRSEL 459
Cdd:pfam12128  891 RLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
PTZ00121 PTZ00121
MAEBL; Provisional
 107-458 4.00e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEHHKALDEKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGS 186
Cdd:PTZ00121  1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED---ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  187 iDSTDDTSQIVELQELLE-KQNYEMAQMKERLTALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIRECYLQAMAQKED 265
Cdd:PTZ00121  1170 -RKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARK---AEDAKKAEAVKKAEEAKKDAEEAKKA 1245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  266 MEERITTLEKRYLSAQRESTSIHDMNDKLENelANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 345
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  346 RIAALTKAEERHGNIEERMRHLE---GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE-RLQLHLKERMAAL 421
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEED 1403

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1327850359  422 EEKNVLIQESENFRKNLEESLHDKE--RLAEEIEKLRSE 458
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEE 1442
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
170-463 4.14e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  170 GMEAGQKVHEKRLSNGSIdSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 249
Cdd:COG4372      1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  250 RDIRecylQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQT 329
Cdd:COG4372     80 EELE----ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  330 MRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNER 409
Cdd:COG4372    156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1327850359  410 LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMK 463
Cdd:COG4372    236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 194-356 4.40e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK-------DLIKTEEMNTKYQ------RDIREcYLQAM 260
Cdd:COG1579     17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKeikrlelEIEEVEARIKKYEeqlgnvRNNKE-YEALQ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDMEERITTLEKRYLsaqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmRKAETLPEVE 340
Cdd:COG1579     96 KEIESLKRRISDLEDEIL--------------ELMERIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAELE 159

                          170
                   ....*....|....*.
gi 1327850359  341 AELAQRIAALTKAEER 356
Cdd:COG1579    160 ELEAEREELAAKIPPE 175
COG5022 COG5022
Myosin heavy chain [General function prediction only];
235-458 5.32e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 47.77  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  235 RKDLIKTEEMNTKYQRDI-RECYLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndklenelanKEAILRQMEEKNR 313
Cdd:COG5022    809 RKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRSLKAK-----------------KRFSLLKKETIYL 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  314 QLQERLELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQRE 385
Cdd:COG5022    872 QSAQRVELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYV 951

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  386 KmNEEHNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSE 458
Cdd:COG5022    952 K-LPELNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKEL 1021
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
348-463 5.36e-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: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  348 AALTKAEERHGNIEER-----MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLK-----ER 417
Cdd:COG2433    380 EALEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSearseER 458

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1327850359  418 MAALEEKNVLIQESENfrKNLEESLHDKErlaEEIEKLRSELDQMK 463
Cdd:COG2433    459 REIRKDREISRLDREI--ERLERELEEER---ERIEELKRKLERLK 499
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 6-468 6.03e-05

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: 47.51  E-value: 6.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359    6 MNTVSGSPKVHLPNGT--RFYTFQ-EFAALTKELNACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LV 71
Cdd:pfam10174   99 TSPVDGEDKFSTPELTeeNFRRLQsEHERQAKELFLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGE 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   72 SRHERSLRMTVVKRQAQspsgvssEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALrEQNVH 151
Cdd:pfam10174  179 EDWERTRRIAEAEMQLG-------HLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL-ERNIR 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  152 ---IQRKMVSSEGSTES----EHLEGMEAgQKVHEKRLSNgSIDSTDD-----TSQIVELQ---ELLEKQNYEMAQ---- 212
Cdd:pfam10174  251 dleDEVQMLKTNGLLHTedreEEIKQMEV-YKSHSKFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhiev 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  213 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREC------------YLQAM-------------------A 261
Cdd:pfam10174  329 LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLteekstlageirDLKDMldvkerkinvlqkkienlqE 408

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  262 QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 340
Cdd:pfam10174  409 QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQ 488

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  341 AELAQRIAALTKAEERHGN-------IEERMRHLEGQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVD 400
Cdd:pfam10174  489 PELTEKESSLIDLKEHASSlassglkKDSKLKSLEIAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVA 568

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  401 RLLTESN------ERLQLHLKE----------RMAALEE-------------KNVLIQESENFRKN---LEESLHDK--- 445
Cdd:pfam10174  569 RYKEESGkaqaevERLLGILREvenekndkdkKIAELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnl 648

                          570       580       590
                   ....*....|....*....|....*....|..
gi 1327850359  446 ---------ERLAEEIEKLRSELDQMKMRTGS 468
Cdd:pfam10174  649 adnsqqlqlEELMGALEKTRQELDATKARLSS 680
PRK11281 PRK11281
mechanosensitive channel MscK;
263-469 6.63e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 6.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 341
Cdd:PRK11281    38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  342 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 419
Cdd:PRK11281   113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1327850359  420 ALEEKNVLIQESENFRKNLEESlhDKERLAEEIEKLRSELD----QMKMRTGSL 469
Cdd:PRK11281   164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQAllnaQNDLQRKSL 215
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 829-893 1.01e-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: 41.49  E-value: 1.01e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  829 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 893
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1037-1107 1.20e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359 1037 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1107
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
PRK12705 PRK12705
hypothetical protein; Provisional
 313-510 1.23e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.24  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  313 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 392
Cdd:PRK12705    26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  393 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHD--KERLAEEIEKLRSELD-QMKMR 465
Cdd:PRK12705    98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1327850359  466 TGSLIEPTISRTHIDTSTELRYSVgslVDSQSDYRTTKVIRRPRR 510
Cdd:PRK12705   178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 198-468 1.34e-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: 46.10  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  198 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITT 272
Cdd:COG5185    272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 338
Cdd:COG5185    352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  339 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 414
Cdd:COG5185    432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1327850359  415 KERMAALEEKNVLIQESENFRKNLEESLHDKERlaEEIEKLRSELDQMKMRTGS 468
Cdd:COG5185    509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 293-463 1.87e-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: 44.53  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  293 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 372
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  373 E-KNQELQRARQREKmnEEHNKRLSDTVDRLLtesnerlqlhlkERMAALEEKNVLIQESENFRKNLEESL-HDKERLAE 450
Cdd:COG1579     84 NvRNNKEYEALQKEI--ESLKRRISDLEDEIL------------ELMERIEELEEELAELEAELAELEAELeEKKAELDE 149

                          170
                   ....*....|...
gi 1327850359  451 EIEKLRSELDQMK 463
Cdd:COG1579    150 ELAELEAELEELE 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-296 2.00e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVE-------VLKA 102
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE---LEAELErldassdDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEHLEGM--EAGQKVHEK 180
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR----LEAAEDLARLELRALLEERfaAALGDAVER 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  181 RLSNGSIDSTDD-TSQIVELQELLEKQnyeMAQMKERLTALSSRVG-EVEQEAETARK-DLIKTEEMnTKYQRDIREcyl 257
Cdd:COG4913    766 ELRENLEERIDAlRARLNRAEEELERA---MRAFNREWPAETADLDaDLESLPEYLALlDRLEEDGL-PEYEERFKE--- 838

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1327850359  258 qamAQKEDMEERITTLeKRYLSAQRES--TSIHDMNDKLEN 296
Cdd:COG4913    839 ---LLNENSIEFVADL-LSKLRRAIREikERIDPLNDSLKR 875
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 119-538 2.15e-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: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  119 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEK--RLSNGSID----STDD 192
Cdd:COG5192    363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 TSQIVELQELLEKQNYEMAQMKERLTALS-SRVGEVEQE---AETARKDLIKTEemNTKYQRDIREC-YLQAMAQKEDME 267
Cdd:COG5192    440 ENEDVDFTGKKGAINNEDESDNEEVAFDSdSQFDESEGNlrwKEGLASKLAYSQ--SGKRGRNIQKIfYDESLSPEECIE 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  268 ERittlekrylsaQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQr 346
Cdd:COG5192    518 EY-----------KGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK- 582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  347 iAALTKAEERHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-- 424
Cdd:COG5192    583 -DATLDSIEGE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElr 654

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  425 -NVLIQESENFRKN-LEESLHDKERLAEEIEKLRSELDQM---------KMRTGSLIEPTISRTHIDTSTELRYS----V 489
Cdd:COG5192    655 gNFELEERGDPEKKdVDWYTEEKRKIEEQLKINRSEFETMvpesrvvieGYRAGRYVRIVLSHVPLEFVDEFNSRypivL 734

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327850359  490 GSLVDSQSDYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGV 538
Cdd:COG5192    735 GGLLPAEKEMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPV 781
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
198-384 2.19e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 45.45  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  198 ELQELLEKQNyEMAQMKERLT-------ALSSRVGEVEQ-EAEtaRKDLIKTEEMntkyQRDIRECYlQAMAQKED-MEE 268
Cdd:COG0497    173 ELEELRADEA-ERARELDLLRfqleeleAAALQPGEEEElEEE--RRRLSNAEKL----REALQEAL-EALSGGEGgALD 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  269 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPE 338
Cdd:COG0497    245 LLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLA 324

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1327850359  339 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 384
Cdd:COG0497    325 YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 235-462 2.71e-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: 45.12  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  235 RKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYlsaQRESTSIHDMND---KLENELANKEAILRQMEEK 311
Cdd:pfam05557    1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQKrirLLEKREAEAEEALREQAEL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  312 NRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEKNQELQRARQR------- 384
Cdd:pfam05557   78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQSTNSELEELQERldllkak 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  385 ----EKMNEEHNKRLSdtvdrLLTESNERLQ----------------LHLKERMAALEEKNVLIQESENFRKNLEESLHD 444
Cdd:pfam05557  148 aseaEQLRQNLEKQQS-----SLAEAEQRIKelefeiqsqeqdseivKNSKSELARIPELEKELERLREHNKHLNENIEN 222

                          250
                   ....*....|....*...
gi 1327850359  445 KERLAEEIEKLRSELDQM 462
Cdd:pfam05557  223 KLLLKEEVEDLKRKLERE 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 98-276 2.89e-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: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   98 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLEGMEAGQKV 177
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-----LEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  178 HEKRLsnGSIDSTDdtsqivELQELLEkqnyEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYL 257
Cdd:COG1579     78 YEEQL--GNVRNNK------EYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145

                          170
                   ....*....|....*....
gi 1327850359  258 QAMAQKEDMEERITTLEKR 276
Cdd:COG1579    146 ELDEELAELEAELEELEAE 164
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 198-430 3.15e-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: 43.94  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  198 ELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYlQAMAQKEDMEERITTLEKR- 276
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAK-ELAEAIKNLIDNIKEINEKv 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  277 -YLSAQRESTSihdmNDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAee 355
Cdd:pfam06008  106 aTLGENDFALP----SSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA-- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  356 rhgnIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKN 425
Cdd:pfam06008  174 ----LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAAN 249


                   ....*
gi 1327850359  426 VLIQE 430
Cdd:pfam06008  250 LLLQE 254
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 27-462 3.20e-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: 45.17  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACRE---QLLEKEEEISELKAERNNT----RLLLEHLECLVSRHERSLRMTVVKRQAQSPSgvSSEVEV 99
Cdd:pfam01576  254 EETAQKNNALKKIREleaQISELQEDLESERAARNKAekqrRDLGEELEALKTELEDTLDTTAAQQELRSKR--EQEVTE 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  100 LKalKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIV-------ALREQNVHIQRKMVS-SEGSTESEHlegm 171
Cdd:pfam01576  332 LK--KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAnlekakqALESENAELQAELRTlQQAKQDSEH---- 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  172 eaGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEmaqmkerLTALSSRVGEVEQEAETARKDLIKTEEmntkYQRD 251
Cdd:pfam01576  406 --KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE-------LESVSSLLNEAEGKNIKLSKDVSSLES----QLQD 472

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  252 IRECYLQAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENELANKEAILRQMEEKNRQLQErlelAEQKLQQTMR 331
Cdd:pfam01576  473 TQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAG 538

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  332 KAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvDRLLTESN 407
Cdd:pfam01576  539 TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF----DQMLAEEK 614

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  408 ERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQM 462
Cdd:pfam01576  615 AISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-320 3.37e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   40 REQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRmtvvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKvRE 119
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALE----AELDALQ-----ERREALQRLAEYSWDEIDVASAEREIAELEAE-LE 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  120 RLRVSLERVSALEEELAAANQEIVALREQnvhiQRKMVSSEGSTESEhLEGMEAGQKVHEKRLSNGSIDSTDDTSQivEL 199
Cdd:COG4913    679 RLDASSDDLAALEEQLEELEAELEELEEE----LDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRA--LL 751

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  200 QELLEKQNYEmAQMKERLTALSSRVGEVEQEAETARKDLIKTeeMNTkYQRDIRECYLQAMAQKEDMEE---RITTLEKR 276
Cdd:COG4913    752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA--MRA-FNREWPAETADLDADLESLPEylaLLDRLEED 827

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1327850359  277 YLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 320
Cdd:COG4913    828 GLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 316-454 3.47e-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: 41.91  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  316 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 395
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850359  396 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 454
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 78-621 4.59e-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: 44.65  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   78 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMV 157
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  158 SSEGSTESEHLEgmeagqkVHEKRLSNGSidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVG------EVEQEA 231
Cdd:TIGR00606  294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  232 ETARKDLIKTEEMNTK---YQRDI---RECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 305
Cdd:TIGR00606  363 IRARDSLIQSLATRLEldgFERGPfseRQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  306 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 385
Cdd:TIGR00606  443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  386 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENF--RKNLEESLH----DKERLAEEIEKLRSEL 459
Cdd:TIGR00606  522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  460 DQMKMRTGSLIEPTISRTHIDTSTELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 537
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  538 VLGSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 617
Cdd:TIGR00606  681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755


                   ....
gi 1327850359  618 VSLE 621
Cdd:TIGR00606  756 VNRD 759
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 830-888 4.92e-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: 39.62  E-value: 4.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327850359  830 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 888
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 225-480 5.86e-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: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  225 GEVEQEAETARKDLIKTEE--MNTKYQRDIRECYLQAMAQKEDMEERITTLEKRYLSAQREstsihDMNDKLENELANKE 302
Cdd:pfam02463  142 GKIEIIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-----KEQAKKALEYYQLK 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  303 AILRQMEEKNRQLQERLELAEQK---------LQQTMRKAETLPEVEAELAQRIAALTKAEER-HGNIEERMRHLEGQLE 372
Cdd:pfam02463  217 EKLELEEEYLLYLDYLKLNEERIdllqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKeKKLQEEELKLLAKEEE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  373 EKNQELQRARQREKMNEEhNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEI 452
Cdd:pfam02463  297 ELKSELLKLERRKVDDEE-KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375

                          250       260
                   ....*....|....*....|....*...
gi 1327850359  453 EKLRSELDQMKMRTGSLIEPTISRTHID 480
Cdd:pfam02463  376 LAKKKLESERLSSAAKLKEEELELKSEE 403
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 226-456 6.58e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 6.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  226 EVEQEAET-----ARKDLIKTEEMNTKYQRDIRECyLQAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMND 292
Cdd:PRK04778    90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDIEQI-LEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALD 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  293 KLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE----------- 355
Cdd:PRK04778   169 ELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyh 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  356 -RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQES 431
Cdd:PRK04778   249 lDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNS 312

                          250       260
                   ....*....|....*....|....*
gi 1327850359  432 ENFRKNLEESLHDKERLAEEIEKLR 456
Cdd:PRK04778   313 DTLPDFLEHAKEQNKELKEEIDRVK 337
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-303 6.72e-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: 43.60  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMvssegSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTS 194
Cdd:COG4942     58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL-----EAQKEELAELLRALYRLGRQPPLALLLSPEDFL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRecylQAMAQKEDM----EERI 270
Cdd:COG4942    133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE----ALKAERQKLlarlEKEL 208

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1327850359  271 TTLEKRYLSAQRESTSIHDMNDKLENELANKEA 303
Cdd:COG4942    209 AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 292-466 7.08e-04

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: 42.43  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  292 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 359
Cdd:cd00176     10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  360 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 429
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1327850359  430 ESENFRKNLEESLH--DKERLAEEIEKLRSELDQMKMRT 466
Cdd:cd00176    164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 115-463 7.87e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.58  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMVSSEGSTESEHlEGMEAGQKVHEKRLSNGsiDSTDDTS 194
Cdd:pfam05557   44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLK--NELSELR 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQEL-LEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQA--MAQKEDMEE--- 268
Cdd:pfam05557  118 RQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdSEIVKNSKSela 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  269 RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------TM 330
Cdd:pfam05557  198 RIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglNL 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  331 RKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNERL 410
Cdd:pfam05557  276 RSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRRV 348

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  411 QLHLKERmaaleekNVLIQESENFRKNLEESLHDkERLAEEIEKLRSELDQMK 463
Cdd:pfam05557  349 LLLTKER-------DGYRAILESYDKELTMSNYS-PQLLERIEEAEDMTQKMQ 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 100-337 7.92e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  100 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesEHLEGMEAGQKVHE 179
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  180 KRLSNgSIDSTDDTSQIVELQELLEKQNyeMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQrdirecylqa 259
Cdd:COG4942    104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE---------- 170

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  260 mAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 337
Cdd:COG4942    171 -AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
mukB PRK04863
chromosome partition protein MukB;
105-395 8.87e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 8.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  105 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHE 179
Cdd:PRK04863   797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  180 KRLSNGSIDSTDDTSQIVELQELLEkQNYEMAQMKERLTALSSRVGEVEQEAETARKDliktEEMNTKYQRDirecYLQA 259
Cdd:PRK04863   877 LNRLLPRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQD----YQQA 947

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  260 MAQKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMR 331
Cdd:PRK04863   948 QQTQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327850359  332 KAETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 395
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 ...
 40-378 8.92e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   40 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 111
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  112 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmvSSEGSTESEHLEGMEAG 174
Cdd:pfam10174  405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  175 QKVHEKRLSNGSIDSTDDTSQIVELQE--------------LLEKQNYEMAQMKERLTALSSRVGEVEQEAETARK---- 236
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpei 556

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  237 -DLIKTEEMNTKYQRD-----------IRECYLQAMAQKEDMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAI 304
Cdd:pfam10174  557 nDRIRLLEQEVARYKEesgkaqaeverLLGILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGA 635

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327850359  305 LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 378
Cdd:pfam10174  636 QLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 199-465 9.66e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.35  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  199 LQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIRECYLQAMAQKEDMEErittLEKRYL 278
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEE----LEEKYK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  279 SAQRESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RH 357
Cdd:pfam07888  105 ELSASSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaER 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  358 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQES 431
Cdd:pfam07888  174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKV 253

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1327850359  432 ENFRKNLEESLHDKERLAEEIEKLRSELDQMKMR 465
Cdd:pfam07888  254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 292-459 1.07e-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: 41.97  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  292 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 360
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  361 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEn 433
Cdd:pfam04012  117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187

                          170       180
                   ....*....|....*....|....*.
gi 1327850359  434 FRKNLEESLHDKERLAEEIEKLRSEL 459
Cdd:pfam04012  188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 27-166 1.20e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   27 QEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgVSSEVEVLKALKSL 106
Cdd:COG1579     31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA---LQKEIESLKRRISD 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  107 FEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESE 166
Cdd:COG1579    108 LE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 416-474 1.20e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.51  E-value: 1.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  416 ERMAALEEKNV-LIQESENFRKNLEESLHDKERLAEEIEKLRSELDqmKMRTGSLIEPTI 474
Cdd:PRK03992     1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELE--KLKSPPLIVATV 58
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 128-460 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  128 VSALEEELAAANQEIVALREQnvhiqrkmvssegsteSEHLEGMEAGQKVHEKRLSngsidstDDTSQIVELQE------ 201
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQER----------------LDQLESGDDSGTPGGKKYL-------LLQKQLEQLQEenfrle 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  202 -----------LLEKQNYEMAQMKERLTAL-----------------SSRVGEVEQEAETARKdliKTEEMN-----TKY 248
Cdd:pfam05622   80 tarddyrikceELEKEVLELQHRNEELTSLaeeaqalkdemdilresSDKVKKLEATVETYKK---KLEDLGdlrrqVKL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  249 QRDIRECYLQAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQK 325
Cdd:pfam05622  157 LEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQkekERLIIERDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  326 LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT-VDRLLT 404
Cdd:pfam05622  237 LRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAE--IREKLIRLQHENKMLRLGQEGSYRERLTeLQQLLE 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327850359  405 ESNER-----------------LQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELD 460
Cdd:pfam05622  315 DANRRkneletqnrlanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
Caldesmon pfam02029
Caldesmon;
118-458 1.31e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  118 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGM-EAGQKVHEKRLSngSIDSTDDTSQI 196
Cdd:pfam02029   12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFlDRTAKREERRQK--RLQEALERQKE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  197 VELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEERITTLEKR 276
Cdd:pfam02029   89 FDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  277 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALT 351
Cdd:pfam02029  169 VPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQ 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  352 KAEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQES 431
Cdd:pfam02029  249 KLEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQE 303

                          330       340
                   ....*....|....*....|....*..
gi 1327850359  432 ENFRKNLEEslHDKERLAEEIEKLRSE 458
Cdd:pfam02029  304 EAERKLREE--EEKRRMKEEIERRRAE 328
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 213-463 1.47e-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: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  213 MKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRECYLQAMAQKEDME-------ERITTLEKRYL----SAQ 281
Cdd:pfam05483  160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhEKIQHLEEEYKkeinDKE 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  282 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERH 357
Cdd:pfam05483  240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDL 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  358 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESENF 434
Cdd:pfam05483  320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKF 399

                          250       260
                   ....*....|....*....|....*....
gi 1327850359  435 RKNLEESLHDKERLAEEIEKLRSELDQMK 463
Cdd:pfam05483  400 KNNKEVELEELKKILAEDEKLLDEKKQFE 428
Caldesmon pfam02029
Caldesmon;
113-419 1.55e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.55  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  113 LDEKVRERLRVSLERVSALEEELAAANqEIVALREQNVHIQRKmvssEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDD 192
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEK-ESVAERKENNEEEEN----SSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  193 TSQIVELQELLEKQNYEMAQMKERLTAlssRVGEVEQEAETARKDLIKTEEMNTKYQRDiRECYLQAMAQKEDMEERITT 272
Cdd:pfam02029  146 STEVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVFLDQK-RGHPEVKSQNGEEEVTKLKV 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  273 LEKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaalt 351
Cdd:pfam02029  222 TTKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL-------- 279

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  352 kaEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 419
Cdd:pfam02029  280 --EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 95-216 1.82e-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: 42.37  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALE---EELAAANQEIVALREQNVHIQRKMvssegsteSEHLEG- 170
Cdd:pfam05622  301 SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKL--------EEHLEKl 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1327850359  171 MEAGQKVHEKRLSNGSIDSTDDTS---QIVELQELLEKQNYEMAQMKER 216
Cdd:pfam05622  373 HEAQSELQKKKEQIEELEPKQDSNlaqKIDELQEALRKKDEDMKAMEER 421
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 200-382 2.08e-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: 40.89  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  200 QELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLikteEMNTKYQRDIRECylqamaqkEDMEERITTLEKRYLS 279
Cdd:cd00176     64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA--------DDLEQWLEEKEAALAS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  280 aqrestsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGN 359
Cdd:cd00176    132 ------------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEE 190

                          170       180
                   ....*....|....*....|...
gi 1327850359  360 IEERMRHLEGQLEEKNQELQRAR 382
Cdd:cd00176    191 LNERWEELLELAEERQKKLEEAL 213
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 104-457 2.10e-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: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  104 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMVSSEGSTESEHLEGMEAGQKVHEKR 181
Cdd:pfam09731  121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  182 LSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAE-TARKDLIKTEEMNTKYQRDIRECYLQAM 260
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELVSIFPDIIPVLKEDNL 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDME-------ERITTLEKR--------YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 325
Cdd:pfam09731  280 LSNDDLNsliahahREIDQLSKKlaelkkreEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  326 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSDtVDRL 402
Cdd:pfam09731  358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK-LNEL 418

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  403 LTESNERLQLhLKERMAALEEKN---VLIQESENFRKNLEESLHDKER--LAEEIEKLRS 457
Cdd:pfam09731  419 LANLKGLEKA-TSSHSEVEDENRkaqQLWLAVEALRSTLEDGSADSRPrpLVRELKALKE 477
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
959-1014 2.19e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  959 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1014
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
206-440 2.21e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  206 QNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREcyLQAMAQKEDMEERITTLEKRYLSAQREst 285
Cdd:COG3206    159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAE-- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  286 sihdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMR 365
Cdd:COG3206    235 -------------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327850359  366 HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEE 440
Cdd:COG3206    295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 115-361 2.27e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  115 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehlegmeagqkvhekrlsngsidstddtS 194
Cdd:COG3883     26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  195 QIVELQELLEKQNyemAQMKERLTAL---SSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIRECYLQAMAQKEDMEER 269
Cdd:COG3883     73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESF-SDFLDRLSALSKIADADADLLEELKADKAELEAK 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  270 ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 349
Cdd:COG3883    149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228

                          250
                   ....*....|..
gi 1327850359  350 LTKAEERHGNIE 361
Cdd:COG3883    229 AAAAAAAAAAAA 240
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
 172-345 2.29e-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: 41.96  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  172 EAGQKVHEKRLSNG---SIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLI-----KTEE 243
Cdd:TIGR03007  179 AAENRLKAFKQENGgilPDQEGDYYSEISEAQEELEAARLELNEAIAQRDALKRQLGGEEPVLLAGSSVANseldgRIEA 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  244 MNTKYQrDIRECYLQAMAQKEDMEERITTLEKRYLSA-------QRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ 316
Cdd:TIGR03007  259 LEKQLD-ALRLRYTDKHPDVIATKREIAQLEEQKEEEgsaknggPERGEIANPVYQQLQIELAEAEAEIASLEARVAELT 337

                          170       180
                   ....*....|....*....|....*....
gi 1327850359  317 ERLElaeqklqQTMRKAETLPEVEAELAQ 345
Cdd:TIGR03007  338 ARIE-------RLESLLRTIPEVEAELTQ 359
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 305-418 2.46e-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: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  305 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 383
Cdd:COG0542    413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  384 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 418
Cdd:COG0542    493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
244-463 2.74e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.60  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  244 MNTKYQRDIrecyLQAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAE 323
Cdd:COG0497    138 LDPDAQREL----LDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEA 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  324 QKLQqtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVD 400
Cdd:COG0497    201 AALQ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAE 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  401 RL------LTESNERLQLHLK------ERMAALEEK-----------NVLIQESENFRKNLEESLHDKERLAEEIEKLRS 457
Cdd:COG0497    269 RLesalieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEA 348


                   ....*.
gi 1327850359  458 ELDQMK 463
Cdd:COG0497    349 ELAEAE 354
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 103-378 2.79e-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: 42.13  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKrl 182
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  183 sngsidstDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETaRKDLIKTE-----EMNTKYQRDIRECYL 257
Cdd:pfam12128  337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIKEQnnrdiAGIKDKLAKIREARD 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  258 QAMAQKEDMEERITTLEKRYLSAQRESTSIhdmnDKLENELANKEAILRQ--------MEEKNRQLQERLELAEQKLQQT 329
Cdd:pfam12128  408 RQLAVAEDDLQALESELREQLEAGKLEFNE----EEYRLKSRLGELKLRLnqatatpeLLLQLENFDERIERAREEQEAA 483

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1327850359  330 MRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 378
Cdd:pfam12128  484 NAEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 203-398 2.93e-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: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  203 LEKQNYEMAQMKERLTALSSRVGE-VEQEAETARKDLIKTEEMNtkyqrDIREcYLQAMAQK----EDMEERITTLEKRY 277
Cdd:cd07666     14 LTAQAWELSSHKKQGPGLLSRMGQtVKAVASSVRGVKNRPEEFT-----EMNE-YVEAFSQKinvlDKISQRIYKEQREY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  278 LSAQRESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAE 342
Cdd:cd07666     88 FEELKEYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAE 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327850359  343 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 398
Cdd:cd07666    165 LDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 19-471 3.00e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   19 NGTRFYTFQEFAALTKELNACREQLLEKEEEISELK----AERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSgVS 94
Cdd:pfam02463  235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlkenKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD-DE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   95 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAG 174
Cdd:pfam02463  314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  175 QKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEaETARKDLIKTEEMNTKYQRDIRe 254
Cdd:pfam02463  394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE-KEELEKQELKLLKDELELKKSE- 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  255 cylqAMAQKEDMEERITTLEKRYLSAQRESTSihdMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAE 334
Cdd:pfam02463  472 ----DLLKETQLVKLQEQLELLLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  335 TLPEVEAELAQRIAALTKAEERHGNIEER---MRHLEGQLEEKNQELQR--------ARQREKMNEEHNKRLSDTVDRLL 403
Cdd:pfam02463  545 ISTAVIVEVSATADEVEERQKLVRALTELplgARKLRLLIPKLKLPLKSiavleidpILNLAQLDKATLEADEDDKRAKV 624

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  404 TESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKERLAEEIEKLRSELDQMKMRTGSLIE 471
Cdd:pfam02463  625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
RNase_Y_N pfam12072
RNase Y N-terminal region;
313-453 3.45e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  313 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 376
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  377 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEnfrknlEESLHDKERLAEEIE 453
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 297-609 3.46e-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: 41.65  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  297 ELANKEAILRQMEEKNRQLQERLELAEQklqQTMRKAETlpeveaelaQRIAALTKAEERHGniEERMRHLEG-QLEEKN 375
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEA---EKARQAEM---------DRQAAIYAEQERMA--MERERELERiRQEERK 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  376 QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHL----------KERMAALEEKNVLIQ----ESENFRKNL--- 438
Cdd:pfam17380  360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaarkvkileEERQRKIQQQKVEMEqiraEQEEARQREvrr 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  439 --EESLHDKERLAEE-------IEKLRSELDQMKMRTGSLIEPTISRTHIDtstELRYSVgslVDSQSDYRTTKVIRRPR 509
Cdd:pfam17380  440 leEERAREMERVRLEeqerqqqVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKI---LEKELEERKQAMIEEER 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  510 RGRMGVRRDEPKVKSLGDHEWNRTQQigvlgshpfesDTEMSDIDDDDRETIFSSMDLLSPSghsdaqtlammlQEQLDA 589
Cdd:pfam17380  514 KRKLLEKEMEERQKAIYEEERRREAE-----------EERRKQQEMEERRRIQEQMRKATEE------------RSRLEA 570

                          330       340
                   ....*....|....*....|
gi 1327850359  590 INKEIRLIQEEKESTELRAE 609
Cdd:pfam17380  571 MEREREMMRQIVESEKARAE 590
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 185-372 3.61e-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: 40.82  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  185 GSIDSTDDTSQIVELQELLEKQNYEMAQM---------KERLTALSSRVGEVEQEAETARKDLikteemnTKYQRDIrec 255
Cdd:cd22656     82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  256 ylqaMAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 333
Cdd:cd22656    152 ----EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLI 224

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1327850359  334 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 372
Cdd:cd22656    225 ADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 835-892 4.16e-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: 4.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327850359  835 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 892
Cdd:cd09487      2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
mukB PRK04863
chromosome partition protein MukB;
30-382 4.56e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   30 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspsgvssevEVL 100
Cdd:PRK04863   782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELE 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  101 KALKSLFEHHKaldeKVRERLRVSLERVSALEEELAAANqeivaLREQNVHIQRKMVSSEGSTESEhlegmEAGQKV--H 178
Cdd:PRK04863   851 RALADHESQEQ----QQRSQLEQAKEGLSALNRLLPRLN-----LLADETLADRVEEIREQLDEAE-----EAKRFVqqH 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  179 EKRLSN-----GSIDStdDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEA-ETARKDLIKTEEMNTKyqrdI 252
Cdd:PRK04863   917 GNALAQlepivSVLQS--DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEK----L 990

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  253 RECYLQAMAQKEDMEERITTLE-------KRYLSAQRESTSIHDMNDKLENELankEAILRQMEEknrQLQERLELAEQK 325
Cdd:PRK04863   991 RQRLEQAEQERTRAREQLRQAQaqlaqynQVLASLKSSYDAKRQMLQELKQEL---QDLGVPADS---GAEERARARRDE 1064

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  326 LQQTMRKAETlpeveaelaqRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRAR 382
Cdd:PRK04863  1065 LHARLSANRS----------RRNQL---EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 198-395 4.86e-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: 40.79  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  198 ELQELLEKQNYEMAQMKERLTALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIREcylQAMAQKEDMEERITTLEKRY 277
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRRE---KQVIEKESRWREQAEDQENQ 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  278 LSAQRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAE 334
Cdd:pfam15558  107 RQEKLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVL 186

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327850359  335 TLPEVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 395
Cdd:pfam15558  187 VDCQAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-355 5.80e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359   98 EVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEeLAAANQEIVALREQNVHIQRkmvssegstESEHLEGMEAGQKV 177
Cdd:COG4913    222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  178 HEKRlsngsidstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQ---EAETARKDLIKTE-EMNTKYQRDIR 253
Cdd:COG4913    291 ELLE------------AELEELRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREiERLERELEERE 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  254 ECYLQAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 333
Cdd:COG4913    359 RRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435

                          250       260
                   ....*....|....*....|..
gi 1327850359  334 ETLPEVEAELAQRIAALTKAEE 355
Cdd:COG4913    436 SNIPARLLALRDALAEALGLDE 457
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-454 6.10e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  103 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEgstesehlegmeagqkvhekrl 182
Cdd:COG4372     15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---------------------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  183 sngsidstddtSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLiktEEMNTKYQrdirecylQAMAQ 262
Cdd:COG4372     73 -----------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL---EELQKERQ--------DLEQQ 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  263 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVE 340
Cdd:COG4372    131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAEQALDELLKEANRNAEKEEELAEAEKLIE 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  341 AELAQRIAALT--KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 418
Cdd:COG4372    211 SLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1327850359  419 AALEEKNVLIQESENFRKNLEESLHDKERLAEEIEK 454
Cdd:COG4372    291 AALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
PRK09039 PRK09039
peptidoglycan -binding protein;
261-382 6.96e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  261 AQKEDMEERITTLEKRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVE 340
Cdd:PRK09039    74 QGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327850359  341 AELAQRIAAL--------TKAEERHGNIEERMRHLEGQLEEKNQELQRAR 382
Cdd:PRK09039   147 AALRRQLAALeaaldaseKRDRESQAKIADLGRRLNVALAQRVQELNRYR 196
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 959-1003 7.22e-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: 36.51  E-value: 7.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1327850359  959 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1003
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 194-350 7.71e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 7.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  194 SQIVELQELLEKQNYEMA-------QMKERLTALSSRVGEVEQEAETARKDliKTEEMNTKYQRDIRECYLQAMA-QKED 265
Cdd:pfam13851   33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKD--KQSLKNLKARLKVLEKELKDLKwEHEV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  266 MEERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV 339
Cdd:pfam13851  111 LEQRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDV 189

                          170
                   ....*....|.
gi 1327850359  340 EAELAQRIAAL 350
Cdd:pfam13851  190 LESKNQLIKDL 200
PRK12705 PRK12705
hypothetical protein; Provisional
 297-465 8.25e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 8.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  297 ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 376
Cdd:PRK12705    40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850359  377 EL--QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENfRKNLEESLhdkERLAEEIEK 454
Cdd:PRK12705   120 ELeeLEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA-QNILAQAM---QRIASETAS 195

                          170
                   ....*....|....*..
gi 1327850359  455 LRS------ELDQMKMR 465
Cdd:PRK12705   196 DLSvsvvpiPSDAMKGR 212
 
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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