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Conserved domains on  [gi|333805616|ref|NP_001207403|]
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liprin-alpha-2 isoform c [Homo sapiens]

Protein Classification

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 ...
1089-1160 4.25e-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: 153.63  E-value: 4.25e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1089 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1160
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 ...
880-950 7.00e-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: 153.10  E-value: 7.00e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805616  880 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 950
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 ...
1004-1069 1.30e-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: 1.30e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616 1004 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1069
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
PRK02224 super family cl32023
DNA double-strand break repair Rad50 ATPase;
41-570 3.49e-16

DNA double-strand break repair Rad50 ATPase;


The actual alignment was detected with superfamily member PRK02224:

Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 83.94  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   41 ERDRLLD------TLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQ-EFAALTKELNACREQLLEKEEEISELKAER 113
Cdd:PRK02224  150 DRQDMIDdllqlgKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQR 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  114 NNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAA 193
Cdd:PRK02224  230 EQARETRDEADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELqellekqnyemaqmKERL 273
Cdd:PRK02224  294 ERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDA 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  274 AALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANK 353
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  354 EAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQ 431
Cdd:PRK02224  425 REREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  432 RARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLR 508
Cdd:PRK02224  500 RAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  509 SELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 570
Cdd:PRK02224  579 SKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAE---LNDERRERLAEKRE 634
 
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 ...
1089-1160 4.25e-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: 153.63  E-value: 4.25e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1089 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1160
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 ...
880-950 7.00e-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: 153.10  E-value: 7.00e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805616  880 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 950
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 ...
1004-1069 1.30e-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: 1.30e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616 1004 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1069
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
41-570 3.49e-16

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 83.94  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   41 ERDRLLD------TLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQ-EFAALTKELNACREQLLEKEEEISELKAER 113
Cdd:PRK02224  150 DRQDMIDdllqlgKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQR 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  114 NNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAA 193
Cdd:PRK02224  230 EQARETRDEADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELqellekqnyemaqmKERL 273
Cdd:PRK02224  294 ERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDA 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  274 AALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANK 353
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  354 EAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQ 431
Cdd:PRK02224  425 REREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  432 RARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLR 508
Cdd:PRK02224  500 RAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  509 SELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 570
Cdd:PRK02224  579 SKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAE---LNDERRERLAEKRE 634
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
251-523 2.52e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 330
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  331 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 410
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  411 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 490
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465
                         250       260       270
                  ....*....|....*....|....*....|...
gi 333805616  491 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-463 2.80e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    80 ALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevevlkAL 159
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------------------QL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   160 KSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESEHLEGMEPGQKVHEKRLS 239
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   240 NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 319
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   320 ERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQR 398
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRR 973
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   399 IAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERL 462
Cdd:TIGR02168  974 LKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENF 1045

                   .
gi 333805616   463 Q 463
Cdd:TIGR02168 1046 Q 1046
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1003-1067 7.08e-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: 67.29  E-value: 7.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  1003 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-521 3.11e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.22  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQEFAALTKELNACREQL-LEKEEE------ 105
Cdd:pfam15921  328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKREKELsLEKEQNkrlwdr 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   106 -------ISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL- 177
Cdd:pfam15921  407 dtgnsitIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELt 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   178 --RVSLER----VSAL-------EEELAAANQEIVALREQnvhIQRKMASSEG-STESEHLEGMEPGQKVHEKRLSngsi 243
Cdd:pfam15921  486 akKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR---VDLKLQELQHlKNEGDHLRNVQTECEALKLQMA---- 558
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   244 dstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 322
Cdd:pfam15921  559 ----EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK 634
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   323 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAA 401
Cdd:pfam15921  635 VKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNT 714
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   402 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQ 481
Cdd:pfam15921  715 LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQ 776
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 333805616   482 ESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 521
Cdd:pfam15921  777 ELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
880-946 6.06e-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: 53.45  E-value: 6.06e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616    880 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 946
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1012-1067 1.25e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.25e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616   1012 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1090-1161 7.71e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 7.71e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616   1090 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1161
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
882-946 1.29e-04

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   882 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 946
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1090-1160 1.58e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616  1090 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1160
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
344-518 6.78e-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: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  344 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 411
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  412 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 481
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 333805616  482 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 518
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
1089-1160 4.25e-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: 153.63  E-value: 4.25e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1089 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1160
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 ...
880-950 7.00e-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: 153.10  E-value: 7.00e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805616  880 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 950
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 ...
1004-1069 1.30e-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: 1.30e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616 1004 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1069
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 ...
1008-1067 2.69e-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: 116.86  E-value: 2.69e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616 1008 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1067
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 ...
887-945 3.96e-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: 105.00  E-value: 3.96e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616  887 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 945
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 ...
1097-1158 8.34e-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: 98.38  E-value: 8.34e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1097 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1158
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 ...
1089-1160 1.42e-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: 1.42e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1089 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1160
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 ...
881-945 6.01e-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: 76.34  E-value: 6.01e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  881 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 945
Cdd:cd09564     2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
1003-1067 1.90e-16

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 74.75  E-value: 1.90e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616 1003 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:cd09567     1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
1003-1067 1.94e-16

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 74.65  E-value: 1.94e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616 1003 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
41-570 3.49e-16

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 83.94  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   41 ERDRLLD------TLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQ-EFAALTKELNACREQLLEKEEEISELKAER 113
Cdd:PRK02224  150 DRQDMIDdllqlgKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQR 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  114 NNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAA 193
Cdd:PRK02224  230 EQARETRDEADEVLEEHEERR----------------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELqellekqnyemaqmKERL 273
Cdd:PRK02224  294 ERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDA 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  274 AALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANK 353
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  354 EAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQ 431
Cdd:PRK02224  425 REREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  432 RARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNVLIQESETFRKNLEESLHDKERLAEEIEKLR 508
Cdd:PRK02224  500 RAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  509 SELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTtkvIRRPRRGRMGVRRD 570
Cdd:PRK02224  579 SKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAE---LNDERRERLAEKRE 634
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
251-523 2.52e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdiREAMAQKEDMEERITTLEKRYL 330
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  331 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRIAALTKAEERHG 410
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  411 NIEERMRHLEGQLEEKNQELQRARQREkmnEEHNKRLSDTVDRLLTESNERLQLHLKERmAALEEKNVLIQESETFRKNL 490
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465
                         250       260       270
                  ....*....|....*....|....*....|...
gi 333805616  491 EESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
1089-1160 2.63e-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: 71.72  E-value: 2.63e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1089 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1160
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-463 2.80e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    80 ALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspsgvssevevlkAL 159
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------------------QL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   160 KSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESEHLEGMEPGQKVHEKRLS 239
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   240 NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 319
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   320 ERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQTMRKAETLPEVEAELAQR 398
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRR 973
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   399 IAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDRLltesNERL 462
Cdd:TIGR02168  974 LKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----NENF 1045

                   .
gi 333805616   463 Q 463
Cdd:TIGR02168 1046 Q 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
249-516 3.02e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 3.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   249 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 328
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   329 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 408
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   409 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 484
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270
                   ....*....|....*....|....*....|..
gi 333805616   485 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 516
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-511 3.24e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 3.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQ---------EFAALTKELN----ACREQLLEKEEEI 106
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeleELEAELEELEsrleELEEQLETLRSKV 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   107 SELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSLERVSA 186
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLEEALEE 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   187 LEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEGMEPGQK--VHEKRLSNG---------SIDSTDET------ 249
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGilgvlseliSVDEGYEAaieaal 543
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   250 ------------SQIVELQELLEKQNYEMAQMKE----RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR------- 306
Cdd:TIGR02168  544 ggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllg 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   307 ------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQERLEL 373
Cdd:TIGR02168  624 gvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAE 702
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   374 AEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 449
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616   450 ---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 511
Cdd:TIGR02168  783 eieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
270-523 4.50e-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: 80.87  E-value: 4.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   270 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 349
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   350 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 422
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   423 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 492
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|.
gi 333805616   493 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
245-517 6.11e-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: 6.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   245 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 324
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   325 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 404
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   405 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 483
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270
                   ....*....|....*....|....*....|....
gi 333805616   484 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
156-509 1.08e-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: 79.33  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   156 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 235
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   236 KRlsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 315
Cdd:TIGR02168  780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   316 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 395
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   396 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 475
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 333805616   476 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRS 509
Cdd:TIGR02168  987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
96-515 2.06e-14

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 78.57  E-value: 2.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    96 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 175
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   176 RLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETSQIVEL 255
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHSRIPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   256 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYlsaqre 335
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK------ 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   336 stsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGNIEER 415
Cdd:TIGR02169  864 --------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEALEEE 932
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   416 MRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETFRKNLE 491
Cdd:TIGR02169  933 LSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVLKRLD 989
                          410       420
                   ....*....|....*....|....*..
gi 333805616   492 ESLHDKERLAEE---IEKLRSELDQLK 515
Cdd:TIGR02169  990 ELKEKRAKLEEErkaILERIEEYEKKK 1016
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1003-1067 7.08e-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: 67.29  E-value: 7.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  1003 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
164-523 1.50e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  164 EHHKALDEKVRER-LRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngs 242
Cdd:COG1196   213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------------------------- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  243 idstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 322
Cdd:COG1196   267 -------AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  323 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 402
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  403 TKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNvliqe 482
Cdd:COG1196   420 EEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA----- 491
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 333805616  483 setfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:COG1196   492 ----RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-515 2.24e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   272 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 351
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   352 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 427
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   428 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 505
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
                          250
                   ....*....|
gi 333805616   506 KLRSELDQLK 515
Cdd:TIGR02168  465 ELREELEEAE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
251-521 3.15e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 74.71  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 330
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   331 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 410
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   411 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 489
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
                          250       260       270
                   ....*....|....*....|....*....|..
gi 333805616   490 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 521
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-517 6.93e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 6.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA------LPQEFAALTKELNACREQLLEKEEEISELKAER 113
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEEELEELEEELEEAEEEL 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  114 NNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVsLERVSALEEELAA 193
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL-EEELEELEEALAE 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYE------MA 267
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvKA 512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  268 QMKERLAALSSRVGEVEQEAETARKDLIKTEE---MNTKYQRDIREAMAQ----KEDMEERITTLEKRyLSAQRESTSIH 340
Cdd:COG1196   513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaaLQNIVVEDDEVAAAAieylKAAKAGRATFLPLD-KIRARAALAAA 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  341 DMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLE 420
Cdd:COG1196   592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  421 GQLEEKNQELQRARQRE-KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKER 499
Cdd:COG1196   672 AALLEAEAELEELAERLaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
                         490       500
                  ....*....|....*....|....
gi 333805616  500 LAEE------IEKLRSELDQLKMR 517
Cdd:COG1196   752 ALEElpeppdLEELERELERLERE 775
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
880-944 1.69e-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: 63.40  E-value: 1.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616  880 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 944
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
302-513 1.89e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  302 TKYQRDIREAMAQKEDMEERIT-------TLEKRY--LSAQRESTSIHdmnDKLENELANKEAILRQMEEknRQLQERLE 372
Cdd:COG1196   168 SKYKERKEEAERKLEATEENLErledilgELERQLepLERQAEKAERY---RELKEELKELEAELLLLKL--RELEAELE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  373 LAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 452
Cdd:COG1196   243 ELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805616  453 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 513
Cdd:COG1196   320 ELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
237-521 4.09e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 70.87  E-value: 4.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   237 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 316
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   317 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 396
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   397 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 476
Cdd:TIGR02169  800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 333805616   477 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 521
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
39-513 5.26e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.48  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLnSALPQEFAALTKELNACREQLLEKEEEISELKAER---NN 115
Cdd:PRK03918  157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELI-KEKEKELEEVLREINEISSELPELREELEKLEKEVkelEE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  116 TRLLLEHLECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSaLEEELAAAN 195
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  196 QEIVALREQNVHIQRKMasSEGSTESEHLEGMEPGQKVHEKRLSngsidstdETSQIVELQELLEKQNYEMAQMKERLAA 275
Cdd:PRK03918  314 KRLSRLEEEINGIEERI--KELEEKEERLEELKKKLKELEKRLE--------ELEERHELYEEAKAKKEELERLKKRLTG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  276 LSsrVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK---RYLSAQRESTSIHDMN--DKLENEL 350
Cdd:PRK03918  384 LT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHRKEllEEYTAEL 461
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  351 ANKEAILRQMEEKNRQLQERLELAEQKLQQ-----TMRK-AETLPEVEAELAQ-RIAALTKAEERHGNIEERMRHLEGQL 423
Cdd:PRK03918  462 KRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKElAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEI 541
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  424 EEKNQELQRARQREKMNEEHNKRLsDTVDRLLTESNERLQLHLKERMAALEEKnvlIQESETFRK---NLEESLHDKERL 500
Cdd:PRK03918  542 KSLKKELEKLEELKKKLAELEKKL-DELEEELAELLKELEELGFESVEELEER---LKELEPFYNeylELKDAEKELERE 617
                         490
                  ....*....|...
gi 333805616  501 AEEIEKLRSELDQ 513
Cdd:PRK03918  618 EKELKKLEEELDK 630
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
151-442 8.12e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 70.10  E-value: 8.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   151 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGM 227
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   228 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 307
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   308 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 387
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   388 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 442
Cdd:TIGR02169  461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
247-523 8.87e-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: 70.09  E-value: 8.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   247 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 319
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   320 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 399
Cdd:TIGR02168  337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   400 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 477
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 333805616   478 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
42-439 1.14e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 69.03  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   42 RDRLLDTLRETQESLSLAQQRL-QDVIYDRDSLQRQLNSA--LPQEFAALTKELNACREQLLEKEEEISELKAERNNTRL 118
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKpELNLKELKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  119 LLEHLECLVSRHE------------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSA 186
Cdd:COG4717   124 LLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  187 LEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEgmepgQKVHEKRLS-------------NGSIDSTDETSQ-- 251
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERLKEARLLlliaaallallglGGSLLSLILTIAgv 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  252 -------IVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 324
Cdd:COG4717   279 lflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  325 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQR 398
Cdd:COG4717   359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEEL 437
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 333805616  399 IAALTKAEERHGNIEERMRHLEGQLE--EKNQELQRARQREKM 439
Cdd:COG4717   438 EEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEE 480
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-517 2.62e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.17  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   49 LRETQESLSLAQQRLQDVIYDRDSLQRQLnsalpQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvs 128
Cdd:PRK03918  202 LEEVLREINEISSELPELREELEKLEKEV-----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK---- 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  129 RHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHI 208
Cdd:PRK03918  273 KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  209 QRKMASSEGSTES-EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGE 282
Cdd:PRK03918  351 EKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEE 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  283 VEQE-----------AETARKDLIK--TEEMNtKYQRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN- 348
Cdd:PRK03918  431 LKKAkgkcpvcgrelTEEHRKELLEeyTAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKEl 508
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  349 ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EG 421
Cdd:PRK03918  509 EEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVE 588
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  422 QLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL--LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE- 498
Cdd:PRK03918  589 ELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEy 661
                         490       500
                  ....*....|....*....|....*..
gi 333805616  499 --------RLAEEIEKLRSELDQLKMR 517
Cdd:PRK03918  662 eelreeylELSRELAGLRAELEELEKR 688
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-521 3.11e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.22  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQEFAALTKELNACREQL-LEKEEE------ 105
Cdd:pfam15921  328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKREKELsLEKEQNkrlwdr 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   106 -------ISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERL- 177
Cdd:pfam15921  407 dtgnsitIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELt 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   178 --RVSLER----VSAL-------EEELAAANQEIVALREQnvhIQRKMASSEG-STESEHLEGMEPGQKVHEKRLSngsi 243
Cdd:pfam15921  486 akKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR---VDLKLQELQHlKNEGDHLRNVQTECEALKLQMA---- 558
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   244 dstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 322
Cdd:pfam15921  559 ----EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK 634
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   323 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAA 401
Cdd:pfam15921  635 VKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNT 714
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   402 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERMAALEEKNVLIQ 481
Cdd:pfam15921  715 LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKHFLKEEKNKLSQ 776
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 333805616   482 ESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 521
Cdd:pfam15921  777 ELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-453 3.66e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 3.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   32 EQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQEFAALTKELNACREQLLEKEEEISELKA 111
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLE 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  112 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHH--KALDEKVRERLRVSLERVSALEE 189
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleAALAAALQNIVVEDDEVAAAAIE 564
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  190 ELAAANQEIVALREQNvhiqrKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQM 269
Cdd:COG1196   565 YLKAAKAGRATFLPLD-----KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  270 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 349
Cdd:COG1196   640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  350 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNI-----------EERMRH 418
Cdd:COG1196   720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEERYDF 799
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 333805616  419 LEGQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDR 453
Cdd:COG1196   800 LSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
50-433 5.93e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   50 RETQESLSLAQQRLQdvIYDRDSLQRQLNSALpQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLeclvsr 129
Cdd:COG1196   216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  130 heRSLRMTVVKRQAQSPSGVSSEVEVLKALkslfehhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQ 209
Cdd:COG1196   287 --QAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  210 RKMASSEGSTESEHLEgmepgQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAET 289
Cdd:COG1196   358 AELAEAEEALLEAEAE-----LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  290 ARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQE 369
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616  370 RLELAEQKLQQtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 433
Cdd:COG1196   513 ALLLAGLRGLA--GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
86-522 7.09e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   86 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 162
Cdd:PRK03918  168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  163 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNGS 242
Cdd:PRK03918  240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSEF---YEEYLDELREIE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  243 IDSTDETSQIVELQELLEKqnyemaqmkerLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERI 322
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  323 T-----TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEV 391
Cdd:PRK03918  382 TgltpeKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEY 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  392 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMA 471
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLI 535
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805616  472 ALEEKnvliqesetfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 522
Cdd:PRK03918  536 KLKGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-409 8.81e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.62  E-value: 8.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    39 LDERDRLLDTLrETQESLSLAQQRLQD--------VIYDR-DSLQRQLnSALPQEFAALTKELNACREQLLEKEEEISEL 109
Cdd:TIGR02168  195 LNELERQLKSL-ERQAEKAERYKELKAelrelelaLLVLRlEELREEL-EELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   110 KAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKaldekvrERLRVSLERvsaLEE 189
Cdd:TIGR02168  273 RLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQK-------QILRERLAN---LER 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   190 ELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetSQIVELQELLEKQNYEMAQM 269
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELE---------------------------------EKLEELKEELESLEAELEEL 363
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   270 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRyLSAQRESTSIHDMnDKLENE 349
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAEL-KELQAE 441
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   350 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 409
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
247-512 2.19e-10

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: 64.32  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   247 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 326
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   327 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 406
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   407 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 472
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 333805616   473 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 512
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
PTZ00121 PTZ00121
MAEBL; Provisional
91-496 3.49e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   91 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 170
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  171 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDE 248
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  249 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 328
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 399
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  400 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 476
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
                         410       420
                  ....*....|....*....|
gi 333805616  477 nvLIQESETFRKNLEESLHD 496
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
mukB PRK04863
chromosome partition protein MukB;
174-521 4.41e-10

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 64.59  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  174 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 250
Cdd:PRK04863  278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 328
Cdd:PRK04863  356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 407
Cdd:PRK04863  415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  408 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 485
Cdd:PRK04863  494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 333805616  486 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 521
Cdd:PRK04863  566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
38-404 6.43e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.93  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNsALPQEFAALTKELNACREQLLEKEEEISELKAErnntr 117
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----- 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   118 llLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAAN 195
Cdd:TIGR02169  760 --LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   196 QEIVALREQNVHIQRKMASSEGSTESEhlegmepGQKVHEKRLsngsidstdetsQIVELQELLEKQNYEMAQMKERLAA 275
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG------------KKEELEEELEELEAALRDLESRLGD 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   276 LSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMnDKLENELAN 352
Cdd:TIGR02169  887 LKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQR 962
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 333805616   353 KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 404
Cdd:TIGR02169  963 VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
51-514 7.33e-10

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 63.45  E-value: 7.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    51 ETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQEFAALTKELN---ACREQLLEKEEEISELKAERNNtrlLLEHLECLV 127
Cdd:TIGR00618  430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVVLARLL---ELQEEPCPL 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   128 srhERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALdEKVRERLRVSLERVSALEEELAAANQEIVALREQnvh 207
Cdd:TIGR00618  507 ---CGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSE-EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC--- 578
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   208 iqrkmassegstESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEA 287
Cdd:TIGR00618  579 ------------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALK 644
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   288 ETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRYLSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KN 364
Cdd:TIGR00618  645 LTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEY 716
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   365 RQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTKAEERHGNIEER----------MRHLEGQLEEKNQELQR 432
Cdd:TIGR00618  717 DREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREE 796
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   433 ARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELD 512
Cdd:TIGR00618  797 DTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876

                   ..
gi 333805616   513 QL 514
Cdd:TIGR00618  877 KL 878
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
157-521 8.41e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  157 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIvalrEQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEK 236
Cdd:PRK03918  162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKEL----EEVLREINEISSELPELREE-LEKLEKEVKELEE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  237 RlsngsidstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR---E 310
Cdd:PRK03918  236 L-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfyeE 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  311 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqqt 381
Cdd:PRK03918  305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL--- 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  382 mrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDR 453
Cdd:PRK03918  382 --TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTA 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  454 LLTESNERLQ-LHLKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQLKM 516
Cdd:PRK03918  460 ELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKG 539

                  ....*
gi 333805616  517 RTGSL 521
Cdd:PRK03918  540 EIKSL 544
PTZ00121 PTZ00121
MAEBL; Provisional
30-523 1.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQEFAALTKELNACREQLLEKEEEISEL 109
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  110 KAERNNTRLLLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR---------ERL 177
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaaakkkaDEA 1423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  178 RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVE--- 254
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeak 1503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  255 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--------DLIKTEEMntKYQRDIREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALR 1581
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  327 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 397
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  398 RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMAALEEkn 477
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKIKAEE-- 1734
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 333805616  478 vLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:PTZ00121 1735 -AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
250-442 1.19e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 61.77  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  250 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaqKEDMEERITTLEKRY 329
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  330 LSAQR------------ESTSIHDMNDKLEN----ELANKEAILRQMEEKNR--QLQERLELAEQKLQQTMRKAET-LPE 390
Cdd:COG3883    93 RALYRsggsvsyldvllGSESFSDFLDRLSAlskiADADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAE 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333805616  391 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 442
Cdd:COG3883   173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-520 1.23e-09

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: 62.83  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    38 MLDERDRLLDTLRETQESLSLAQQRLQDV--------------------------------------------------- 66
Cdd:pfam15921  122 MQMERDAMADIRRRESQSQEDLRNQLQNTvheleaakclkedmledsntqieqlrkmmlshegvlqeirsilvdfeeasg 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    67 --IYDRDSLQ----RQLNSALPQEFAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRHERSL- 134
Cdd:pfam15921  202 kkIYEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEIt 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   135 ----RMTVVKRQAQSpsgVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEI 198
Cdd:pfam15921  282 glteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   199 VALReqnvhIQRKMASSEGSTESEHLEGMEPGQKVHEKRLS-----NGSIDSTDETSQIV--ELQELLEKQNYEMAQMKE 271
Cdd:pfam15921  359 TEAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEVQRLEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   272 RLAALSSRV-GEVEQEAETARKdliKTEEMNtKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLEnel 350
Cdd:pfam15921  434 LLKAMKSECqGQMERQMAAIQG---KNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ--- 506
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   351 aNKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEERHGNIE 413
Cdd:pfam15921  507 -EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQHGRTA 585
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   414 ERMR----HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHlKERMAAL----EEKNVLIQESET 485
Cdd:pfam15921  586 GAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG-SERLRAVkdikQERDQLLNEVKT 664
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 333805616   486 FRKNLEESLHDKERLAEEI----EKLRSELDQLKMRTGS 520
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKS 703
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
266-677 1.34e-09

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: 62.83  E-value: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   266 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 345
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   346 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 419
Cdd:pfam15921  304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   420 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 475
Cdd:pfam15921  376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   476 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTK 555
Cdd:pfam15921  456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITK 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   556 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 632
Cdd:pfam15921  522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 333805616   633 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 677
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
305-520 1.58e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 61.32  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  305 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 384
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  385 AETLpevEAELAQRIAALTK------------------AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:COG4942    99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616  447 LSDTVDRLLTEsNERLQLHLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGS 520
Cdd:COG4942   176 LEALLAELEEE-RAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
247-667 1.72e-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: 62.39  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   247 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 326
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   327 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 406
Cdd:TIGR02169  232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   407 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 485
Cdd:TIGR02169  298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   486 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 565
Cdd:TIGR02169  345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   566 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 643
Cdd:TIGR02169  409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
                          410       420
                   ....*....|....*....|....
gi 333805616   644 KEIRLIQEEKESTELRAEEIENRV 667
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERV 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
81-511 2.11e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   81 LPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALK 160
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  161 SLFEHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMASSEGST 219
Cdd:PRK03918  392 ELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKE 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  220 ESEHLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIK 296
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEK 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  297 TEEMNTKyqrdIREAMAQKEDMEERITTLEKRYLSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQL 367
Cdd:PRK03918  551 LEELKKK----LAELEKKLDELEEELAELLKELEELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKKL 624
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  368 QERLELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNK 445
Cdd:PRK03918  625 EEELDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELE 686
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616  446 RLSDTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 511
Cdd:PRK03918  687 KRREEIKKTLEK--------LKEELEEREKA---KKELE----KLEKALERVEELREKVKKYKALL 737
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
39-510 2.45e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   39 LDERDRLLDTLR--ETQESLSLAQQRLQDVIYDRDSLQRQLnSALPQEFAALTKELNACREQLLEKE-EEISELKAERNN 115
Cdd:COG4913   271 LAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAEL-ERLEARLDALREELDELEAQIRGNGgDRLEQLEREIER 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  116 TRLLLEHLECLVSRHERSLRMTvvkrQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAAN 195
Cdd:COG4913   350 LERELEERERRRARLEALLAAL----GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  196 QEIVALRE------QNVHIQRKMASSE-GSTES------EHLEgMEPGQKV---------------------HEKRLSNg 241
Cdd:COG4913   426 AEIASLERrksnipARLLALRDALAEAlGLDEAelpfvgELIE-VRPEEERwrgaiervlggfaltllvppeHYAAALR- 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  242 SIDSTDETSQIVELQELLEKQNYEMAQMKER-LAA-LSSRVGEVEQEAE---TARKDLIK---TEEMN------------ 301
Cdd:COG4913   504 WVNRLHLRGRLVYERVRTGLPDPERPRLDPDsLAGkLDFKPHPFRAWLEaelGRRFDYVCvdsPEELRrhpraitragqv 583
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  302 ----TKYQRDIREAMAQK----EDMEERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLEL 373
Cdd:COG4913   584 kgngTRHEKDDRRRIRSRyvlgFDNRAKLAALEAEL--------------AELEEELAEAEERLEALEAELDALQERREA 649
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  374 AEQKLQQTMRKAEtLPEVEAELA---QRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 450
Cdd:COG4913   650 LQRLAEYSWDEID-VASAEREIAeleAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616  451 VDRLLT-------ESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSE 510
Cdd:COG4913   729 LDELQDrleaaedLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
880-946 6.06e-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: 53.45  E-value: 6.06e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616    880 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 946
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
36-476 7.38e-09

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: 60.12  E-value: 7.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRQLNS--ALPQEFAALTKELNACREqllEKEEEISELKAE 112
Cdd:pfam05483  270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTICQLTE---EKEAQMEELNKA 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   113 RNNTRLLLEHLECLVSRHERSLR------------MTVVKRQAQSPSgvsSEVEVLKALKS-----LFEHHKALDEKvrE 175
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRteqqrleknedqLKIITMELQKKS---SELEEMTKFKNnkeveLEELKKILAED--E 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   176 RLRVSLERVSALEEELAAANQEIVAL---REQNVH---IQ------------RKMASSEGSTESEHLEGMEPGQKVHEKR 237
Cdd:pfam05483  419 KLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQltaiktseehylKEVEDLKTELEKEKLKNIELTAHCDKLL 498
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   238 LSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI-----------KTEEMNTKY 304
Cdd:pfam05483  499 LENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckldKSEENARSI 578
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   305 QRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELANKEAILRQMEEK 363
Cdd:pfam05483  579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQKFEEIIDN 658
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   364 NRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRHLeGQLEEKNQEL 430
Cdd:pfam05483  659 YQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSEL-GLYKNKEQEQ 737
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 333805616   431 QRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAALEEK 476
Cdd:pfam05483  738 SSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAILKDK 786
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
306-517 7.71e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.31  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  306 RDIREAMaqkEDMEERITTLE------KRYLSAQRESTSIHDMNDKLEnelankeaiLRQMEEKNRQLQERLELAEQKLQ 379
Cdd:COG4913   238 ERAHEAL---EDAREQIELLEpirelaERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  380 QTMRKAETLPEVEAELAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrLLTESN 459
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEF 382
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 333805616  460 ERLQLHLKERMAALEEknvliqESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:COG4913   383 AALRAEAAALLEALEE------ELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-538 8.90e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 8.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   257 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 331
Cdd:TIGR02168  203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   332 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 411
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   412 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 491
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 333805616   492 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 538
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
273-521 1.10e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  273 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 350
Cdd:PRK03918  127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  351 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 427
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  428 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 499
Cdd:PRK03918  283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
                         250       260
                  ....*....|....*....|..
gi 333805616  500 LAEEIEKLRSELDQLKMRTGSL 521
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGL 384
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
250-461 1.61e-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: 58.24  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  250 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 329
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  330 ----LSAQREST--------SIHDMNDkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 397
Cdd:COG4942   107 aellRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616  398 RIAALTKAEERHgniEERMRHLEGQLEEKNQELQRARQREkmneehnKRLSDTVDRLLTESNER 461
Cdd:COG4942   186 ERAALEALKAER---QKLLARLEKELAELAAELAELQQEA-------EELEALIARLEAEAAAA 239
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
196-512 1.71e-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: 59.20  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  196 QEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKVHEKRLSNGSI-DSTDETSQIVELQELLEKQNYEMAQMKER 272
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQqlRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  273 LAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRdireAMAQKEDMEERITTLEkrYLSAQRESTSIHD----------M 342
Cdd:COG3096   916 GKALA----QLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdL 985
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  343 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL-----TKAEERhgnIEERMR 417
Cdd:COG3096   986 NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadAEAEER---ARIRRD 1062
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  418 HLEGQL----EEKNQ-ELQRARQREKMnEEHNKRLSDtVDRLLTESNERLQLHLKERMAALEeknvLIQESetfrkNLEE 492
Cdd:COG3096  1063 ELHEELsqnrSRRSQlEKQLTRCEAEM-DSLQKRLRK-AERDYKQEREQVVQAKAGWCAVLR----LARDN-----DVER 1131
                         330       340
                  ....*....|....*....|
gi 333805616  493 SLHDKERLAEEIEKLRSELD 512
Cdd:COG3096  1132 RLHRRELAYLSADELRSMSD 1151
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
33-515 2.12e-08

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: 58.70  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    33 QLMVNMLDERDRLlDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQEFAALTKELNacrEQLLEKEEEISELKAE 112
Cdd:pfam12128  231 QAIAGIMKIRPEF-TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQ-EERQETSAELN---QLLRTLDDQWKEKRDE 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   113 RNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSEVEVL-KALKSLFEHHKALDEKVrERLRvs 180
Cdd:pfam12128  306 LNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKY-NRRR-- 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   181 LERVSALEEELAAANQEIVALREQnvhIQRKMASSEGsteseHLEGME-PGQKVHEKRLSNGSIDSTDETSQIVELQELL 259
Cdd:pfam12128  382 SKIKEQNNRDIAGIKDKLAKIREA---RDRQLAVAED-----DLQALEsELREQLEAGKLEFNEEEYRLKSRLGELKLRL 453
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   260 EKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSI 339
Cdd:pfam12128  454 NQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   340 HDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETL-------------------PEVEAE 394
Cdd:pfam12128  526 ELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLygvkldlkridvpewaaseEELRER 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   395 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKERMA 471
Cdd:pfam12128  606 LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEkdkKNKALAERKDSANERLN 685
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 333805616   472 ALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQLK 515
Cdd:pfam12128  686 SLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK 735
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
37-439 2.41e-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: 57.77  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    37 NMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNsALPQEFAALTKELNACREQLLEKEEEISELKAERNNT 116
Cdd:pfam19220   38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLS-AAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   117 RLLLEHLEclvsrherslrmtvvKRQAQspsgvssEVEVLKALKslfEHHKALdekvRERLRVSLERVSALEEELAAAnQ 196
Cdd:pfam19220  117 TAQAEALE---------------RQLAA-------ETEQNRALE---EENKAL----REEAQAAEKALQRAEGELATA-R 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   197 EIVALREQNVHIQRKMASSEGSTESEHLEGMEPgqkvHEKRLSNGSIDSTDETSQIVELQELLEK----QNYEMAQMKER 272
Cdd:pfam19220  167 ERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERaeaqLEEAVEAHRAE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   273 LAALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELAN 352
Cdd:pfam19220  243 RASLRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   353 KEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEERMRHLEGQ-------LEE 425
Cdd:pfam19220  309 RTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAELTKRfeveraaLEQ 371
                          410
                   ....*....|....
gi 333805616   426 KNQELQRARQREKM 439
Cdd:pfam19220  372 ANRRLKEELQRERA 385
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
78-522 2.92e-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: 58.11  E-value: 2.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    78 NSALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLK 157
Cdd:TIGR04523  161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELK 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   158 ALKSLFEhhKALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHE 235
Cdd:TIGR04523  225 KQNNQLK--DNIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLK 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   236 KRLSNgsIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqK 315
Cdd:TIGR04523  295 SEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----K 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   316 EDMEERIttlekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 395
Cdd:TIGR04523  369 QNEIEKL----------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   396 AQRIAALTKA----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE 457
Cdd:TIGR04523  439 NSEIKDLTNQdsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616   458 SNErlqlhLKERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 522
Cdd:TIGR04523  519 ISS-----LKEKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
251-408 3.87e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.70  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEkqnyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR-- 328
Cdd:COG1579     8 ALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 -------YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAA 401
Cdd:COG1579    84 nvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEE 160

                  ....*..
gi 333805616  402 LTKAEER 408
Cdd:COG1579   161 LEAEREE 167
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
30-474 6.83e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.05  E-value: 6.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN--SALPQEFAALTKELNA-CREQ 98
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrNMEVQRLEALLKAMKSeCQGQ 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    99 LlekEEEISELKAERNNtrllLEHLECLVSRHERS---LRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDE---- 171
Cdd:pfam15921  446 M---ERQMAAIQGKNES----LEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtnae 518
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   172 --KVRERLRVSLERVSALEEE-----------------LAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQK 232
Cdd:pfam15921  519 itKLRSRVDLKLQELQHLKNEgdhlrnvqtecealklqMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   233 VHEKR--LSNGSIDSTDETSQIVELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTEEMNTK 303
Cdd:pfam15921  599 INDRRleLQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLSEDYEV 678
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   304 YQRDIREamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERLELAEQ 376
Cdd:pfam15921  679 LKRNFRN---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEE 755
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   377 KLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMneehnkRLSDTVDRLLT 456
Cdd:pfam15921  756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL------QFAECQDIIQR 829
                          490
                   ....*....|....*...
gi 333805616   457 ESNERLQLHLKERMAALE 474
Cdd:pfam15921  830 QEQESVRLKLQHTLDVKE 847
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
302-515 7.45e-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: 56.99  E-value: 7.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   302 TKYQRDIREAMAQKEDMEERITTLE---------KRYLSAQRESTSI-HDMNDKLENelANKEAILRQMEEKNRQLqERL 371
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEKAERyKELKAELRE--LELALLVLRLEELREEL-EEL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   372 ELAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 450
Cdd:TIGR02168  245 QEELKEAEEELEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   451 VDRL----------LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 515
Cdd:TIGR02168  325 LEELeskldelaeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
151-515 8.15e-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: 56.67  E-value: 8.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   151 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 228
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   229 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 303
Cdd:pfam17380  346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   304 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 383
Cdd:pfam17380  412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   384 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 462
Cdd:pfam17380  463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333805616   463 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 515
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
43-511 8.80e-08

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: 56.77  E-value: 8.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    43 DRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQEFAALTKELNACRE-QLLEKEEEISELKAERNNTRLLLE 121
Cdd:pfam12128  470 DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAGTLLHFLRKEAPDWEQ 549
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   122 HLECLVSR---HERSLRMTVVKRQAQSPS---GVSSEVEVLKALKSLFeHHKALDE---KVRERLRVSLERVSALEEELA 192
Cdd:pfam12128  550 SIGKVISPellHRTDLDPEVWDGSVGGELnlyGVKLDLKRIDVPEWAA-SEEELRErldKAEEALQSAREKQAAAEEQLV 628
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   193 AANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQE--LLEKQNYEMAQM 269
Cdd:pfam12128  629 QAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqLDKKHQAWLEEQ 705
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   270 KERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKL 346
Cdd:pfam12128  706 KEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI 784
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   347 ENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRIAaltKAEERHGNIEERMRHLEGQLEE 425
Cdd:pfam12128  785 ERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQQLARLIA---DTKLRRAKLEMERKASEKQQVR 857
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   426 KNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAALEE-KNVLIQESETFRKNLEE-----SLHDKE 498
Cdd:pfam12128  858 LSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHfknviADHSGS 926
                          490
                   ....*....|...
gi 333805616   499 RLAEEIEKLRSEL 511
Cdd:pfam12128  927 GLAETWESLREED 939
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
97-502 8.83e-08

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.98  E-value: 8.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    97 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 171
Cdd:TIGR00606  684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   172 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNVHIQRKMASSEGSTESEHLEG--MEPGQKVHEKRLS 239
Cdd:TIGR00606  759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   240 NGSIdstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 319
Cdd:TIGR00606  838 LDTV-----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   320 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 399
Cdd:TIGR00606  913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   400 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 476
Cdd:TIGR00606  984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
                          410       420       430
                   ....*....|....*....|....*....|.
gi 333805616   477 NVLIQESETF-----RKNLEESLHDKERLAE 502
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELRE 1093
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
78-516 9.74e-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: 56.72  E-value: 9.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    78 NSALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSlRMTVVKRQAQSPSGVSSEVEVLK 157
Cdd:pfam01576  147 NSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKRKLEGESTDLQEQIA 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   158 ALKSLFEHHKALDEKVRERLRVSLERvsaLEEELAAANQEIVALREQNVHI------------QRKMASSEGSTESEHLE 225
Cdd:pfam01576  226 ELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQIselqedleseraARNKAEKQRRDLGEELE 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   226 GMepgqkvheKRLSNGSIDST--------DETSQIVELQELLEKQ----NYEMAQMKERLAALSSRVGEVEQEAETARKD 293
Cdd:pfam01576  303 AL--------KTELEDTLDTTaaqqelrsKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   294 LIKT----EEMNTKYQRDIREAMAQKEDMEER-------ITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE 362
Cdd:pfam01576  375 LEKAkqalESENAELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   363 KNRQLQERLELAEQKLQQTMrkaETLPEveaELAQRIAALTKAEErhgnIEERMRHLEGQLEEknqELQRARQREKMNEE 442
Cdd:pfam01576  455 KNIKLSKDVSSLESQLQDTQ---ELLQE---ETRQKLNLSTRLRQ----LEDERNSLQEQLEE---EEEAKRNVERQLST 521
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   443 HNKRLSDTVDRLLTESnerlqlhlkERMAALEE-KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 516
Cdd:pfam01576  522 LQAQLSDMKKKLEEDA---------GTLEALEEgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLV 587
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
73-506 1.12e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 56.18  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    73 LQRQlNSALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSE 152
Cdd:TIGR04523  223 LKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   153 VEVLKALKSlfehhKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIqrkmassegstesehlegmepgqk 232
Cdd:TIGR04523  297 ISDLNNQKE-----QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL------------------------ 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   233 vhEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAM 312
Cdd:TIGR04523  348 --KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQ 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   313 AQKEDMEERITTLEKRYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-- 383
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKel 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   384 -----KAETLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTE 457
Cdd:TIGR04523  492 kskekELKKLNEEKKELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNK 568
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 333805616   458 SNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 506
Cdd:TIGR04523  569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
360-515 1.17e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.16  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  360 MEEKNRQLqERLELAEQKLQQTMRKAETLP----EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARq 435
Cdd:COG1579     2 MPEDLRAL-LDLQELDSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  436 rEKMNEEHNKRLSDTVDR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL-HDKERLAEEIEKLRSEL 511
Cdd:COG1579    80 -EQLGNVRNNKEYEALQKeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAEL 158

                  ....
gi 333805616  512 DQLK 515
Cdd:COG1579   159 EELE 162
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1012-1067 1.25e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 1.25e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616   1012 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
250-540 1.45e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  250 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY 329
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  330 LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMrkaetlpevEAELAQRIAALTKAEERH 409
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS---------EAEAEQALDELLKEANRN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  410 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 489
Cdd:COG4372   196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805616  490 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYS 540
Cdd:COG4372   276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
175-523 1.62e-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: 55.75  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   175 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 254
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   255 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 334
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   335 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 408
Cdd:TIGR00618  353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   409 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 469
Cdd:TIGR00618  430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333805616   470 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
174-509 1.74e-07

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 56.11  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  174 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE---------SEHLEGMEPGQKVHEKrlsngsID 244
Cdd:COG3096   277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdleqdyqaaSDHLNLVQTALRQQEK------IE 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  245 STDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 324
Cdd:COG3096   351 RYQE--DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-------ADYQQALDVQQTRAIQYQQAVQA 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  325 LEKrylsaQRESTSIHDMN-DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL----PEVEAELA-QR 398
Cdd:COG3096   422 LEK-----ARALCGLPDLTpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVckiaGEVERSQAwQT 496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  399 IAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDrllteSNERLQLHLKERMAALEEknv 478
Cdd:COG3096   497 ARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----AAEELEELLAELEAQLEE--- 568
                         330       340       350
                  ....*....|....*....|....*....|.
gi 333805616  479 LIQESETFRKNLEESLHDKERLAEEIEKLRS 509
Cdd:COG3096   569 LEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
291-514 1.86e-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: 55.75  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   291 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 366
Cdd:TIGR00618  165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   367 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 437
Cdd:TIGR00618  245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   438 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQ 513
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404

                   .
gi 333805616   514 L 514
Cdd:TIGR00618  405 L 405
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
96-520 2.14e-07

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: 55.21  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    96 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 167
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   168 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPG 230
Cdd:pfam10174  405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   231 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIRE 310
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEE 548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   311 AMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAE 386
Cdd:pfam10174  549 AVRTNPEINDRIRLLEQEVARYKEESG-------KAQAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVA 621
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   387 TLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEGQLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESN 459
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQLQLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLR 696
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616   460 ERLQLHLKERM--------AALEEKNVLIQEsetfrknLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 520
Cdd:pfam10174  697 AERRKQLEEILemkqeallAAISEKDANIAL-------LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-521 2.33e-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: 55.46  E-value: 2.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    41 ERDRLLDTLRETQESLSLAQQRLQDViydrdslqrqlnsalPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLL 120
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEV---------------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   121 EHLECLVSRHERSLRmTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVA 200
Cdd:TIGR02169  416 QRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   201 LREQNVHIQRkmASSEGSTESEHLEGMEPG--------QKVHEK-----------RLSNGSIDsTDETSQivELQELLEK 261
Cdd:TIGR02169  495 AEAQARASEE--RVRGGRAVEEVLKASIQGvhgtvaqlGSVGERyataievaagnRLNNVVVE-DDAVAK--EAIELLKR 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   262 QNY---------EMAQMkERLAALSSRVGEVE--------------------------QEAETARKDLI----------- 295
Cdd:TIGR02169  570 RKAgratflplnKMRDE-RRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvEDIEAARRLMGkyrmvtlegel 648
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   296 --------------KTEEMNTKYQRD-IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQM 360
Cdd:TIGR02169  649 feksgamtggsrapRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   361 EEKNRQLQERLELAEQKLQQTMRKAET----LPEVEAELAQRIAALTKAEERHGNIEERMRHleGQLEEKNQELqrarqr 436
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENvkseLKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL------ 800
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   437 EKMNEEHnKRLSDTVDRLLTESNERLQL--HLKERMAALEEKNVLIQES-ETFRKNLEESLHDKERLAEEIEKLRSELDQ 513
Cdd:TIGR02169  801 SKLEEEV-SRIEARLREIEQKLNRLTLEkeYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRD 879

                   ....*...
gi 333805616   514 LKMRTGSL 521
Cdd:TIGR02169  880 LESRLGDL 887
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
202-514 2.47e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.18  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   202 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 279
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAArQKLQlEKVTTEAKIKKLEEDILLLEDQN--SKLSKERKLLEERISEFTSN 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   280 VGEVEQEAETARKDLIKTEEMNTkyqrDIREAMAQKEDMEERittLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQ 359
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   360 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 429
Cdd:pfam01576  241 KEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   430 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 480
Cdd:pfam01576  321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKANLEKAKQALESENAELqaelrtlqq 398
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 333805616   481 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 514
Cdd:pfam01576  399 akQDSEHKRKKLEGQLQElqarlseserqRAELAEKLSKLQSELESV 445
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
325-517 2.74e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  325 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 404
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  405 AEERHgNIEERMRHLEGQLEE---KNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKErmaaleeknvLIQ 481
Cdd:COG4717   131 YQELE-ALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----------LAE 199
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 333805616  482 ESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:COG4717   200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-435 5.15e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEmnTKYQRDIREAMAQKEDMEERITTLEKRYL 330
Cdd:COG4913   250 QIELLEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  331 SAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQkLQQTMRKAE-TLPEVEAELAQRI----AALTKA 405
Cdd:COG4913   327 ELEAQ---------IRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALGlPLPASAEEFAALRaeaaALLEAL 396
                         170       180       190
                  ....*....|....*....|....*....|
gi 333805616  406 EERHGNIEERMRHLEGQLEEKNQELQRARQ 435
Cdd:COG4913   397 EEELEALEEALAEAEAALRDLRRELRELEA 426
PRK01156 PRK01156
chromosome segregation protein; Provisional
91-463 5.95e-07

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 54.14  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   91 ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 170
Cdd:PRK01156  333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  171 eKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNGSIDSTDETS 250
Cdd:PRK01156  409 -KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHYNEKKSRLEE 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMAQK------E 316
Cdd:PRK01156  484 KIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIKNRykslklE 561
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  317 DMEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNRQLQERLELA 374
Cdd:PRK01156  562 DLDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEANNLNNKYNEI 638
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  375 EQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTV 451
Cdd:PRK01156  639 QENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
                         410
                  ....*....|..
gi 333805616  452 drllTESNERLQ 463
Cdd:PRK01156  719 ----NDINETLE 726
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
187-417 6.15e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.87  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  187 LEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgQKVHEKRLSNGSIDSTDET----SQIVELQELLEKQ 262
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAE--------------AALEEFRQKNGLVDLSEEAklllQQLSELESQLAEA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  263 NYEMAQMKERLAALSSRVGEVEQEAETARKDlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDM 342
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAAL 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  343 NDKLENELankEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMR 417
Cdd:COG3206   304 RAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
86-372 7.10e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   86 AALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgvssevevlkalkslfeh 165
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA--------------------- 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  166 hkALDEKvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDS 245
Cdd:COG4913   672 --ELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-----KELEQAEEELDELQDRLEAAEDLA 743
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  246 TDETSQivELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQRDIREAMAQKEDMEE---R 321
Cdd:COG4913   744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEylaL 820
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333805616  322 ITTLEKRYLSAQREstsihDMNDKL-ENELANKEAILRQMEEKNRQLQERLE 372
Cdd:COG4913   821 LDRLEEDGLPEYEE-----RFKELLnENSIEFVADLLSKLRRAIREIKERID 867
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1090-1161 7.71e-07

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.68  E-value: 7.71e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616   1090 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1161
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-538 8.06e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 8.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  250 SQIVELQELLEKQNYEMAQMKERLAALSSRvGEVEQEAETARKDLIKTEEmntkYQRDIREAMAQKED----------ME 319
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERldassddlaaLE 691
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  320 ERITTLEKRYlsaqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRI 399
Cdd:COG4913   692 EQLEELEAEL--------------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF 755
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  400 AALtKAEERHGNIEERmrhLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDRLLT--ESNERLQLHLK----ERMAA 472
Cdd:COG4913   756 AAA-LGDAVERELREN---LEERIDALRARLNRAEEElERAMRAFNREWPAETADLDAdlESLPEYLALLDrleeDGLPE 831
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616  473 LEEK--NVLIQESETFRKNLEESLHDKERLAEE-IEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 538
Cdd:COG4913   832 YEERfkELLNENSIEFVADLLSKLRRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDPEVREFR 900
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
266-450 8.38e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  266 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND- 344
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  345 --------KLENELANKEAILRQMEEKN---RQLQERLELAEQKLQQTMRKAETL-----PEVEAELAQRIAALTKAEER 408
Cdd:COG4717   128 lplyqeleALEAELAELPERLEELEERLeelRELEEELEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQR 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 333805616  409 HGNIEERMRHLEGQLEEKNQELQRArQREKMNEEHNKRLSDT 450
Cdd:COG4717   208 LAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEA 248
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
226-515 8.79e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  226 GMEPGQKVHEKRLSNGSIdSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ 305
Cdd:COG4372     1 GDRLGEKVGKARLSLFGL-RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  306 RDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 385
Cdd:COG4372    80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  386 ETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLH 465
Cdd:COG4372   160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 333805616  466 LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 515
Cdd:COG4372   240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-404 1.09e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRL 118
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  119 LLEHLECLVSRHERSLRmtvVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKV-----------RERLRVSLERVSAL 187
Cdd:COG4717   228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEA 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  188 EEELAAANQEIVALREQNVHIQRKMASSEGSTEsehlEGMEPGQKVHEKRLSNGSIDSTDETSQIV----ELQELLEKQN 263
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDLSPE----ELLELLDRIEELQELLREAEELEEELQLEeleqEIAALLAEAG 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  264 -------YEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKyqrdiREAMAQKEDMEERITTLEKRYLSAQRES 336
Cdd:COG4717   381 vedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREEL 455
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  337 TSIHDMNDKLEN--ELANKEAILRQMEEKNRQLQER---LELAEQKLQQTMRKA--ETLPEVEAELAQRIAALTK 404
Cdd:COG4717   456 AELEAELEQLEEdgELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYreERLPPVLERASEYFSRLTD 530
PRK12704 PRK12704
phosphodiesterase; Provisional
349-506 1.28e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  349 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 428
Cdd:PRK12704   34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  429 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 505
Cdd:PRK12704  111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179

                  .
gi 333805616  506 K 506
Cdd:PRK12704  180 E 180
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
41-430 1.53e-06

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.52  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    41 ERDRLLDTLRETQESLSLAQQRLQDviydrdslqrqlnsaLPQEFAALTKELNACREQLLEKEEEISELKAERNNtrlLL 120
Cdd:pfam10174  346 EVDALRLRLEEKESFLNKKTKQLQD---------------LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQ 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   121 EHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSLFEhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQE 197
Cdd:pfam10174  408 EQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTLEE---ALSEKERiiERLKEQREREDrERLEELESLKKE 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   198 IVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEK-QNYEMAQMKErlA 274
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--P 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   275 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSaQRESTSIHDMNDKLENELANKE 354
Cdd:pfam10174  555 EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKK 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   355 AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQE 429
Cdd:pfam10174  634 GAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEA 713

                   .
gi 333805616   430 L 430
Cdd:pfam10174  714 L 714
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-365 1.75e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    43 DRLLDTLRETQESLSLAQQR-----LQDVIYDRDSLQRQLnSALPQEFAALTKELNACREQLLEKEEEISELKAERNNT- 116
Cdd:TIGR02169  214 QALLKEKREYEGYELLKEKEalerqKEAIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRv 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   117 RLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEVEVLkaLKSLFEHHKALDEKVRERLRvsleRVSALEEELAAANQ 196
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIA--EKERELEDAEERLAKLEAE--IDKLLAEIEELEREIEEERK----RRDKLTEEYAELKE 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   197 EIVALREQNVHIQRKMASS--EGSTESEHLEGMEpgqkvHEKRLSNGSIDstdetsqivELQELLEKQNYEMAQMKERLA 274
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETrdELKDYREKLEKLK-----REINELKRELD---------RLQEELQRLSEELADLNAAIA 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   275 ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkleneLANKE 354
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE--------------LAEAE 496
                          330
                   ....*....|.
gi 333805616   355 AILRQMEEKNR 365
Cdd:TIGR02169  497 AQARASEERVR 507
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
174-553 3.05e-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: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  174 RERLRVSLERVSALEEELAAANQEIVALR-EQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE------KRLSNGSIDST 246
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIDVASAEREIAeleaelERLDASSDDLA 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  247 DETSQIVELQEllekqnyEMAQMKERLAALSSRVGEVEQEAETArkdlikteemntkyQRDIREAMAQKEDMEERITTLE 326
Cdd:COG4913   689 ALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLEL 747
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  327 KRYLSAQRESTSIhdmnDKLENELAnkeailRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRIAALTKA 405
Cdd:COG4913   748 RALLEERFAAALG----DAVERELR------ENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPEY 817
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  406 EERHGNIEERmrhlegQLEEKNQELQRARQR----------EKMNEEHN---KRLsDTVDRLLTESN----ERLQLHLKE 468
Cdd:COG4913   818 LALLDRLEED------GLPEYEERFKELLNEnsiefvadllSKLRRAIReikERI-DPLNDSLKRIPfgpgRYLRLEARP 890
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  469 RmaALEEKNVLIQE-----SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIepTIPRTHLDTSAELRYSV-G 542
Cdd:COG4913   891 R--PDPEVREFRQElravtSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRARV--LDVRNHLEFDAEEIDREdG 966
                         410
                  ....*....|.
gi 333805616  543 SLVDSQSDYRT 553
Cdd:COG4913   967 EEVETYSSSGG 977
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
45-514 3.88e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.33  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    45 LLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLnsalpqefaaltKELNAcreQLLEKEEEISELKAERNNT----RLLL 120
Cdd:pfam01576  234 LRAQLAKKEEELQAALARLEEETAQKNNALKKI------------RELEA---QISELQEDLESERAARNKAekqrRDLG 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   121 EHLECLVSRHERSLRMTVVKRQAQSPSgvSSEVEVLKalKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIV- 199
Cdd:pfam01576  299 EELEALKTELEDTLDTTAAQQELRSKR--EQEVTELK--KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAn 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   200 ------ALREQNVHIQRKMAS-SEGSTESEHlegmepGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmaqmker 272
Cdd:pfam01576  375 lekakqALESENAELQAELRTlQQAKQDSEH------KRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE------- 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   273 LAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENELAN 352
Cdd:pfam01576  442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED-------ERNSLQEQ---LEEEEEA 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   353 KEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEEKNQ 428
Cdd:pfam01576  512 KRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektkNRLQQELDDLLV 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   429 ELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLR 508
Cdd:pfam01576  588 DLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663

                   ....*.
gi 333805616   509 SELDQL 514
Cdd:pfam01576  664 AEMEDL 669
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
40-277 3.99e-06

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: 50.53  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLN------SALPQEFAALTKELNACREQLLEKEEEISELKAER 113
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  114 NNTRLLLEHLECLVSRHERSLRMTVVKrqaqSPSGVSSEVEVLKALKSLFEHHKALdekvRERLRVSLERVSALEEELAA 193
Cdd:COG4942   100 EAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAALRAELEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREQNVHIQRKMASSEGSTESEhlegmepgQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERL 273
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243

                  ....
gi 333805616  274 AALS 277
Cdd:COG4942   244 PAAG 247
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
246-514 4.78e-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: 50.79  E-value: 4.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   246 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 314
Cdd:TIGR04523   92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   315 KEDMEERITTLEKrylsaqrESTSIHDMNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 390
Cdd:TIGR04523  168 KEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   391 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 470
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 333805616   471 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 514
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
307-484 4.95e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  307 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA- 385
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALy 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  386 ---ETLPEVEA--------ELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 454
Cdd:COG3883    97 rsgGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                         170       180       190
                  ....*....|....*....|....*....|
gi 333805616  455 LTESNERLQLHLKERMAALEEKNVLIQESE 484
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELA 206
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
308-475 5.45e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  308 IREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAeqklqQTMRKAET 387
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----RNNKEYEA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  388 LpevEAELAQriaaltkAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 467
Cdd:COG1579    94 L---QKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163

                  ....*...
gi 333805616  468 ERMAALEE 475
Cdd:COG1579   164 EREELAAK 171
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
247-511 8.52e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 8.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   247 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 322
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   323 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 401
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   402 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 474
Cdd:pfam02463  319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 333805616   475 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 511
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1012-1063 8.95e-06

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.15  E-value: 8.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333805616 1012 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1063
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
251-523 1.17e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 320
Cdd:TIGR04523  132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   321 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 393
Cdd:TIGR04523  212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   394 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 458
Cdd:TIGR04523  292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616   459 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
267-515 1.50e-05

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: 49.35  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   267 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 346
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR------------------ 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   347 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 426
Cdd:pfam05557   64 ---EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA----------ELELQST 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   427 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 506
Cdd:pfam05557  131 NSELEELQER---LDLLKAKASE-----AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201

                   ....*....
gi 333805616   507 LRSELDQLK 515
Cdd:pfam05557  202 LEKELERLR 210
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
347-515 1.54e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  347 ENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK 426
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  427 NQELQRARQREKMNEE--HNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKnvliqesetfRKNLEESLHDKER 499
Cdd:COG3883    92 ARALYRSGGSVSYLDVllGSESFSDFLDRLsalskIADADADLLEELKADKAELEAK----------KAELEAKLAELEA 161
                         170
                  ....*....|....*.
gi 333805616  500 LAEEIEKLRSELDQLK 515
Cdd:COG3883   162 LKAELEAAKAELEAQQ 177
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
180-384 1.94e-05

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.82  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   180 SLERVSALEEELAAANQEIVALREQNVHIQRKmassegstesehlegmepgQKVHEKRLSNgsIDSTDEtsqivELQELL 259
Cdd:pfam15619    9 RLHKIKELQNELAELQSKLEELRKENRLLKRL-------------------QKRQEKALGK--YEGTES-----ELPQLI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   260 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA-MAQKEDMEERITTLEKRYLSAQREsts 338
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEK--- 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333805616   339 IHDMNDKLEN-------ELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK 384
Cdd:pfam15619  140 IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
62-222 1.96e-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: 47.23  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   62 RLQDVIYDRDSLQRQLNSaLPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR 141
Cdd:COG1579    11 DLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  142 QAQSpsgVSSEVEVLKALKSLFEhhkaldekvrERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES 221
Cdd:COG1579    90 EYEA---LQKEIESLKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156

                  .
gi 333805616  222 E 222
Cdd:COG1579   157 E 157
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-517 1.97e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  167 KALDEKVRErLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRlsngsidst 246
Cdd:COG4717    74 KELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALE--------- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  247 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemNTKYQRDIREAMAQKEDMEERITTLE 326
Cdd:COG4717   139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEELQQRLAELE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  327 KRYLSAQREstsihdmNDKLENELANKEAILRQMEEKNRQLQERLELA--------EQKLQQTMRKAETLPEVEAELAQR 398
Cdd:COG4717   213 EELEEAQEE-------LEELEEELEQLENELEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLGL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  399 IAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrLSDTVDRLLTESNERLQLHLKERMAALE 474
Cdd:COG4717   286 LALlfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEE 361
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805616  475 EknVLIQESETFRKNL--------EESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:COG4717   362 E--LQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQ 410
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
337-447 2.78e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  337 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 411
Cdd:PRK00409  509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 333805616  412 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 447
Cdd:PRK00409  589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
172-515 3.23e-05

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: 47.93  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   172 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 248
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   249 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 318
Cdd:pfam06160  154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   319 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 398
Cdd:pfam06160  224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   399 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 465
Cdd:pfam06160  288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 333805616   466 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 515
Cdd:pfam06160  362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
244-516 3.87e-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: 47.89  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   244 DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-EEMNTKYQrdIREAMAQKEDMEERI 322
Cdd:pfam10174  158 ESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ--LQPDPAKTKALQTVI 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   323 TTLEKRYLSAQRestSIHDMNDKLENELAN-------KEAILRQME----------EKNRQLQERLELAEQKLQQTMRKA 385
Cdd:pfam10174  236 EMKDTKISSLER---NIRDLEDEVQMLKTNgllhtedREEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKL 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   386 ETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEE---------HNKRLSDTV 451
Cdd:pfam10174  313 ETLTNQNSDCKQHIevlkESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirDLKDMLDVK 392
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   452 DR---LLTESNERLQLHLKERMAALEEKNVLIQESETFRKN-------LEESLHDKERLAEEIEKLRSELDQLKM 516
Cdd:pfam10174  393 ERkinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRERL 467
PRK01156 PRK01156
chromosome segregation protein; Provisional
41-550 4.17e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   41 ERDRLLDTLRETqESLSLAQQRLQDVI-----------YDRDSLQRQLNsalpqEFAALTKELNACREQLLEKEEEISEL 109
Cdd:PRK01156  150 QRKKILDEILEI-NSLERNYDKLKDVIdmlraeisnidYLEEKLKSSNL-----ELENIKKQIADDEKSHSITLKEIERL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  110 KAERNNTRLLLEHLEclVSRHERSLRMTVVKRQ----AQSPSGVSSEVEVLKALKSLFEHHKALDE----KVRERLRVSL 181
Cdd:PRK01156  224 SIEYNNAMDDYNNLK--SALNELSSLEDMKNRYeseiKTAESDLSMELEKNNYYKELEERHMKIINdpvyKNRNYINDYF 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  182 ERVSALE---EELAAANQEIvalreQNVHIQRKMASSEGSTESEHLEgMEPGQKVHEKRLSNGSIDSTDETSQIVELQEL 258
Cdd:PRK01156  302 KYKNDIEnkkQILSNIDAEI-----NKYHAIIKKLSVLQKDYNDYIK-KKSRYDDLNNQILELEGYEMDYNSYLKSIESL 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  259 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL----IKTEEMNTK---YQRDIREAMAQKEDMEERITTLEKR--- 328
Cdd:PRK01156  376 KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELneinVKLQDISSKvssLNQRIRALRENLDELSRNMEMLNGQsvc 455
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 -----YLSAQRESTSIHDMNDK---LENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQ-- 397
Cdd:PRK01156  456 pvcgtTLGEEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIESARADLEDik 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  398 -RIAALTKAEERHGNIEERMRHLE-GQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNERLQlhlkERMAALE 474
Cdd:PRK01156  536 iKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQ----EIEIGFP 611
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  475 EKNVLIQESETFRKNLEESLHDKERLAEE----IEKLRSELDQLKMRTGSL--IEP---TIPRTHLDTSAELRYSVGSLV 545
Cdd:PRK01156  612 DDKSYIDKSIREIENEANNLNNKYNEIQEnkilIEKLRGKIDNYKKQIAEIdsIIPdlkEITSRINDIEDNLKKSRKALD 691

                  ....*
gi 333805616  546 DSQSD 550
Cdd:PRK01156  692 DAKAN 696
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
156-389 6.10e-05

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: 46.68  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  156 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHE 235
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-----KEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  236 KRLSNgSIDSTDETSQIVELQELLEKQNyeMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 315
Cdd:COG4942   104 EELAE-LLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616  316 EDMEERITTLEKryLSAQRESTSihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 389
Cdd:COG4942   181 AELEEERAALEA--LKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
PRK12705 PRK12705
hypothetical protein; Provisional
365-562 7.08e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  365 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 444
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  445 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 517
Cdd:PRK12705   98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 333805616  518 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 562
Cdd:PRK12705  178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
254-436 8.26e-05

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.61  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  254 ELQELLEKQNyEMAQMKERL-------AALSSRVGEVEQ-EAEtaRKDLIKTEEMNTKYQRdIREAMAQKED-MEERITT 324
Cdd:COG0497   173 ELEELRADEA-ERARELDLLrfqleelEAAALQPGEEEElEEE--RRRLSNAEKLREALQE-ALEALSGGEGgALDLLGQ 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  325 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQ---ERLELAEQKLQ---QTMRK----AETLPEVEAE 394
Cdd:COG0497   249 ALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdpERLEEVEERLAllrRLARKygvtVEELLAYAEE 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 333805616  395 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQR 436
Cdd:COG0497   329 LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
255-517 8.64e-05

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: 46.81  E-value: 8.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   255 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 334
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   335 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 413
Cdd:pfam07888  109 SSEELS----------EEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQ 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   414 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 487
Cdd:pfam07888  178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
                          250       260       270
                   ....*....|....*....|....*....|
gi 333805616   488 KNLEESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:pfam07888  258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
400-523 9.98e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.77  E-value: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  400 AALTKAEERHGNIEErmrhlegqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEknvL 479
Cdd:COG2433   380 EALEELIEKELPEEE---------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-VEELEAELEEKDERIER---L 446
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 333805616  480 IQESETFRKNLEESLH-DKE--RLAEEIEKLRSELDQLKMRTGSLIE 523
Cdd:COG2433   447 ERELSEARSEERREIRkDREisRLDREIERLERELEEERERIEELKR 493
PRK11281 PRK11281
mechanosensitive channel MscK;
315-514 1.24e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.44  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  315 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 393
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  394 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 471
Cdd:PRK11281  113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 333805616  472 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 514
Cdd:PRK11281  164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
882-946 1.29e-04

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   882 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 946
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
171-408 1.32e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  171 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGsidstdeTS 250
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----RRIRALEQELAALEAELAEL-------EK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNYEMAQMKeRLAALSSRVGEVEQ--EAETArKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 328
Cdd:COG4942    91 EIAELRAELEAQKEELAELL-RALYRLGRQPPLALllSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 yLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 408
Cdd:COG4942   169 -LEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
mukB PRK04863
chromosome partition protein MukB;
161-447 1.57e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  161 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 233
Cdd:PRK04863  797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  234 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 313
Cdd:PRK04863  877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  314 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 385
Cdd:PRK04863  950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  386 ETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 447
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1090-1160 1.58e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616  1090 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1160
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
171-413 1.63e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  171 EKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdetS 250
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---------------------------------A 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  251 QIVELQELLEKQNyemAQMKERLAAL---SSRVGEVEQ--EAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERI 322
Cdd:COG3883    73 EIAEAEAEIEERR---EELGERARALyrsGGSVSYLDVllGSESFSDFLDRLSALSKIADADadlLEELKADKAELEAKK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  323 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAAL 402
Cdd:COG3883   150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
                         250
                  ....*....|.
gi 333805616  403 TKAEERHGNIE 413
Cdd:COG3883   230 AAAAAAAAAAA 240
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
308-515 1.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  308 IREAMAQKEDMEERITTLEKRYlsaqresTSIHDMNDKLEnELANKEAILRQMEEKNRQLQE-RLELAEQKLQQTMRKAE 386
Cdd:COG4913   213 VREYMLEEPDTFEAADALVEHF-------DDLERAHEALE-DAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLW 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  387 TLPEVEAELAQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQRekmneehnkRLSDTVDRL--LTESNERLQL 464
Cdd:COG4913   285 FAQRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQ---------IRGNGGDRLeqLEREIERLER 352
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616  465 HLKERMAALEEKNVLIQ--------ESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 515
Cdd:COG4913   353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
272-531 1.95e-04

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: 45.62  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   272 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 333
Cdd:pfam06160   61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   334 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 395
Cdd:pfam06160  141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   396 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 465
Cdd:pfam06160  217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616   466 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQLKMRtgsLIEPTIPRTHL 531
Cdd:pfam06160  294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVER---LEEKEVAYSEL 362
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
182-397 2.26e-04

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: 45.43  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   182 ERVSALEEELAAANQEIVALREQNVhiqrkmassegstesehleGMEPGQkvhekrlsngsidSTDETSQIVELQELLEK 261
Cdd:TIGR03007  168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   262 QNYEMAQMKERLAALSSRVGEVEQEAETARKDL-----IKTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 326
Cdd:TIGR03007  216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805616   327 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 397
Cdd:TIGR03007  296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIASLEARVAELTARIE-------RLESLLRTIPEVEAELTQ 359
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
254-482 2.31e-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: 44.33  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   254 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 333
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   334 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 410
Cdd:pfam06008  105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   411 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 480
Cdd:pfam06008  174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252

                   ..
gi 333805616   481 QE 482
Cdd:pfam06008  253 QE 254
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
81-355 2.51e-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: 44.75  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   81 LPQEFAALTKELNACREQLLEKEEEISELKAERNNTRlllehleclvsrherslrmtvvkrqaqspsgvSSEVEVLKALK 160
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK--------------------------------KEEKALLKQLA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  161 SLfehhkaldekvRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSN 240
Cdd:COG4942    59 AL-----------ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-----AQKEELAELLRALYRLGRQPPL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  241 GSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDM-- 318
Cdd:COG4942   123 ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLla 202
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 333805616  319 --EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEA 355
Cdd:COG4942   203 rlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PTZ00121 PTZ00121
MAEBL; Provisional
68-511 2.87e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   68 YDRDSLQRQLNSALPQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEhleclvSRHERSLRMTVVKRQAQSPS 147
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE------ARKAEDARKAEEARKAEDAK 1152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  148 GVSSEVEVLKALKsLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE-QNVHIQRKMASSEGSTESEHLEG 226
Cdd:PTZ00121 1153 RVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKK 1231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  227 MEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--DLIKTEEMNTKY 304
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKA 1311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  305 Q--RDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmndklenELANKEAilRQMEEKNRQLQERLELAEQKLQQTM 382
Cdd:PTZ00121 1312 EeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------------EAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAK 1377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  383 RKAEtlpeveaELAQRIAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESN--E 460
Cdd:PTZ00121 1378 KKAD-------AAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKkaD 1447
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 333805616  461 RLQLHLKERMAA--LEEKNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSEL 511
Cdd:PTZ00121 1448 EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEA 1502
mukB PRK04863
chromosome partition protein MukB;
56-522 3.30e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   56 LSLAQQRL---QDVIYDRDSLQRQLNSAL--PQEFAALTKELNACREQLlekEEEISELKAERNNTRLLLEHLECLVSRH 130
Cdd:PRK04863  522 LSELEQRLrqqQRAERLLAEFCKRLGKNLddEDELEQLQEELEARLESL---SESVSEARERRMALRQQLEQLQARIQRL 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  131 E------RSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKAL---DEKVRERLRVSLERVSALEEELAAANQEIVAL 201
Cdd:PRK04863  599 AarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELtveRDELAARKQALDEEIERLSQPGGSEDPRLNAL 678
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  202 REQ-----------NVHIQ-------------RKMASSEGSTESEHLEGME--PGqkvhEKRLSNGSIDSTDETSQIVEL 255
Cdd:PRK04863  679 AERfggvllseiydDVSLEdapyfsalygparHAIVVPDLSDAAEQLAGLEdcPE----DLYLIEGDPDSFDDSVFSVEE 754
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  256 QELLEKQNYEMAQMK----------------ERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKED 317
Cdd:PRK04863  755 LEKAVVVKIADRQWRysrfpevplfgraareKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShlAVAFEAD 834
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  318 MEERIttlekRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA-ETLPEVEAELA 396
Cdd:PRK04863  835 PEAEL-----RQLNRRRV---------ELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAdETLADRVEEIR 900
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  397 QRIAALTKAE---ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVdRLLTESNERlQLHLKERMAA- 472
Cdd:PRK04863  901 EQLDEAEEAKrfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQA-FALTEVVQR-RAHFSYEDAAe 978
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805616  473 -LEEKNVLiqeSETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 522
Cdd:PRK04863  979 mLAKNSDL---NEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK 1026
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
254-517 3.55e-04

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: 44.14  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   254 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 329
Cdd:pfam13868   56 ALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   330 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 397
Cdd:pfam13868  136 NEEQAEWKELEKEEEREEDE-RILEYLKEKAEREEEREAEREEIEEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   398 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 472
Cdd:pfam13868  215 qerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 333805616   473 LEEknvLIQESE-TFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 517
Cdd:pfam13868  295 LEK---QIEEREeQRAAEREEELEEGERLREEEAERRERIEEERQK 337
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
175-602 4.46e-04

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


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 44.73  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  175 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 248
Cdd:COG5192   363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  249 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 328
Cdd:COG5192   440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  329 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 407
Cdd:COG5192   516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  408 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 484
Cdd:COG5192   591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  485 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTSaELRYSV--GSLVDSQS 549
Cdd:COG5192   664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEF-NSRYPIvlGGLLPAEK 742
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 333805616  550 DYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 602
Cdd:COG5192   743 EMGIVQGrIKRHRWHKKILKTNDPLIFSVG---WRRFQSIPVYSMKDSRTRNRM 793
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
883-941 5.31e-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: 5.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  883 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 941
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
262-492 5.36e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  262 QNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR--DIREAMAQKEDMEERITTLEKRYLSAQREstsi 339
Cdd:COG3206   159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAE---- 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  340 hdmndklenelankeaiLRQMEEKNRQLQERLELAEQKLQQTMRkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 419
Cdd:COG3206   235 -----------------LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616  420 EGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEE 492
Cdd:COG3206   297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
47-222 5.36e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   47 DTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECL 126
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN-EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  127 VSRHERSLRMTVVKRQAQSPSGVSSEVEVLKAL----KSLFEHHKALDEKV---RERLRVSLERVSALEEELAAANQEIV 199
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIadadADLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAELE 174
                         170       180
                  ....*....|....*....|...
gi 333805616  200 ALREQNVHIQRKMASSEGSTESE 222
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQ 197
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
282-508 5.73e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  282 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 345
Cdd:PRK04778   90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  346 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 407
Cdd:PRK04778  170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  408 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 484
Cdd:PRK04778  250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313
                         250       260
                  ....*....|....*....|....
gi 333805616  485 TFRKNLEESLHDKERLAEEIEKLR 508
Cdd:PRK04778  314 TLPDFLEHAKEQNKELKEEIDRVK 337
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-543 6.55e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  159 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrl 238
Cdd:COG4372    15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---------------------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  239 sngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDM 318
Cdd:COG4372    73 -----------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  319 EERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME--EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELA 396
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSeaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  397 QRIAALT--KAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 474
Cdd:COG4372   215 ELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616  475 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGS 543
Cdd:COG4372   295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
344-518 6.78e-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: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  344 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 411
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  412 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 481
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 333805616  482 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 518
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
249-514 7.16e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  249 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 326
Cdd:PRK04778  111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  327 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 383
Cdd:PRK04778  191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  384 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 454
Cdd:PRK04778  271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616  455 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 514
Cdd:PRK04778  337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
41-272 7.40e-04

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: 43.52  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    41 ERDRLL---DTLRETQESLSLAQqrLQdviydrdslQRQLNSALPQEFAALTKELNACREQL-LEKEEEISELKAErnNT 116
Cdd:pfam05622  226 EKERLIierDTLRETNEELRCAQ--LQ---------QAELSQADALLSPSSDPGDNLAAEIMpAEIREKLIRLQHE--NK 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   117 RLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALE---EELAA 193
Cdd:pfam05622  293 MLRLGQEG--------------------------SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQK 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   194 ANQEIVALREQNVHIQRKM---------ASSEGSTESEHLEGMEPGQkvhekrlsngsidSTDETSQIVELQELLEKQNY 264
Cdd:pfam05622  347 ALQEQGSKAEDSSLLKQKLeehleklheAQSELQKKKEQIEELEPKQ-------------DSNLAQKIDELQEALRKKDE 413

                   ....*...
gi 333805616   265 EMAQMKER 272
Cdd:pfam05622  414 DMKAMEER 421
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
300-515 7.70e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.53  E-value: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  300 MNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsihdmndkLENELANKEAILRQMEEKNRQLQErleLAEQKLQ 379
Cdd:COG0497   138 LDPDAQRELLDAFAGLEELLEEYREAYRAWRALKKE----------LEELRADEAERARELDLLRFQLEE---LEAAALQ 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  380 qtmrkaetlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGqlEEKN--QELQRARQR-EKMnEEHNKRLSDTVDRL-- 454
Cdd:COG0497   205 ---------PGEEEELEEERRRLSNAEKLREALQEALEALSG--GEGGalDLLGQALRAlERL-AEYDPSLAELAERLes 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  455 ----LTESNERLQLHLK------ERMAALEEK-----------NVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 513
Cdd:COG0497   273 alieLEEAASELRRYLDslefdpERLEEVEERlallrrlarkyGVTVEELLAYAEELRAELAELENSDERLEELEAELAE 352

                  ..
gi 333805616  514 LK 515
Cdd:COG0497   353 AE 354
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
250-402 8.49e-04

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   250 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 319
Cdd:pfam13851   33 EEIAELKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   320 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 393
Cdd:pfam13851  113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191

                   ....*....
gi 333805616   394 ELAQRIAAL 402
Cdd:pfam13851  192 SKNQLIKDL 200
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
368-506 9.55e-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: 40.75  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   368 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 447
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616   448 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 506
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
468-526 1.16e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  468 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 526
Cdd:PRK03992    1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
282-515 1.18e-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: 43.17  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   282 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 361
Cdd:pfam05483  201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   362 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 437
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   438 KMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 514
Cdd:pfam05483  348 SFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427

                   .
gi 333805616   515 K 515
Cdd:pfam05483  428 E 428
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
302-515 1.21e-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: 43.42  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   302 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 377
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   378 -----LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRlsdtVD 452
Cdd:pfam02463  244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KL 316
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805616   453 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 515
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
134-673 1.43e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   134 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMA 213
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   214 SSEGSTESEHLEgmepgqkVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEA 287
Cdd:TIGR00606  294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   288 ETARKDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 357
Cdd:TIGR00606  363 IRARDSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   358 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 437
Cdd:TIGR00606  443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   438 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSEL 511
Cdd:TIGR00606  522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   512 DQLKMRTGSLIEPTIPRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 589
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   590 VLSSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 669
Cdd:TIGR00606  681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755

                   ....
gi 333805616   670 VSLE 673
Cdd:TIGR00606  756 VNRD 759
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
338-515 1.50e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  338 SIHDMND---KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK---------AETLPEVEAELAQRIAALTKA 405
Cdd:COG1842    31 AIRDMEEdlvEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  406 EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNeEHNKRLSDTVDRLLTESNErlqlhlkERMAALEEKnvliQESET 485
Cdd:COG1842   111 EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDAT-------SALERMEEK----IEEME 178
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 333805616  486 FRKNLEESLHDKERLAEEIEKLRS------ELDQLK 515
Cdd:COG1842   179 ARAEAAAELAAGDSLDDELAELEAdsevedELAALK 214
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
171-469 1.54e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.81  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   171 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHEKRLSNGSI-DSTDET 249
Cdd:pfam05557   44 DRESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKYLEALNKKLN----EKESQLADAREVISCLkNELSEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   250 SQIVELQEL-LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 320
Cdd:pfam05557  117 RRQIQRAELeLQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   321 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 381
Cdd:pfam05557  197 aRIPELEKE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSwvklaqdtglN 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   382 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 461
Cdd:pfam05557  275 LRSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL----QRR 347

                   ....*...
gi 333805616   462 LQLHLKER 469
Cdd:pfam05557  348 VLLLTKER 355
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-664 1.67e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616    39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQEFAALTKELNA-CREQLLEKEEEISELKAERNNTR 117
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   118 LLLEHLECLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLErvsALEEELAAAN 195
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE---EVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   196 QEIVALREQNVHIQRKMASSEGstesEHLEGMEPGQKVHEkRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAA 275
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKR----ELDRLQEELQRLSE-ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   276 LSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT------------------------TLEKRYLS 331
Cdd:TIGR02169  460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaqlgSVGERYAT 539
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   332 AQRESTSIHDMNDKLENELANKEAILRQMEEK---------NRQLQERLELAEQKLQQTMRKAETLPEVEAELA------ 396
Cdd:TIGR02169  540 AIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyv 619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   397 -------QRIAAltkAEERHGNIeeRMRHLEGQLEEKN---------------------QELQRARQREKMNEEHNKRLS 448
Cdd:TIGR02169  620 fgdtlvvEDIEA---ARRLMGKY--RMVTLEGELFEKSgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQ 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   449 DTVDRLLTESNERLQL--HLKERMAALE-EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEpt 525
Cdd:TIGR02169  695 SELRRIENRLDELSQElsDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-- 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   526 iprthldTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSShpfESDTEMSDI 605
Cdd:TIGR02169  773 -------DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQR 842
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616   606 DD--DDRETIFSSMDLLSPSGHSDAQTLAMM------LQEQLDAINKEIRLIQEEKESTELRAEEIE 664
Cdd:TIGR02169  843 IDlkEQIKSIEKEIENLNGKKEELEEELEELeaalrdLESRLGDLKKERDELEAQLRELERKIEELE 909
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
254-520 1.74e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  254 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETAR-----KDLIKTEEMNTKYQRDIREA----MAQKEDMEERITT 324
Cdd:COG5185   272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETetgiQNLTAEIEQGQES 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  325 LEKRYLSAQRESTSIHDMND------KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPE-------- 390
Cdd:COG5185   352 LTENLEAIKEEIENIVGEVElsksseELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqieq 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  391 VEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQRE--KMNEEHNKRLSDTVDRLLT--ESNERLQLHL 466
Cdd:COG5185   432 ATSSNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSvrSKKEDLNEELTQIESRVSTlkATLEKLRAKL 508
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 333805616  467 KERMAALEEKNVLIQESETFRKNLEESLHDKERlaEEIEKLRSELDQLKMRTGS 520
Cdd:COG5185   509 ERQLEGVRSKLDQVAESLKDFMRARGYAHILAL--ENLIPASELIQASNAKTDG 560
COG5022 COG5022
Myosin heavy chain [General function prediction only];
291-514 1.81e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  291 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 370
Cdd:COG5022   809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  371 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 442
Cdd:COG5022   877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805616  443 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 514
Cdd:COG5022   956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
Caldesmon pfam02029
Caldesmon;
174-510 2.22e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   174 RERLRVSLERVSAlEEELAAANQEIVALREQNVHIQRKMASSEGSTESEH----LEGMEPGQKVHEKRLSNGSIDSTDET 249
Cdd:pfam02029   12 RRRAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQEALERQKEFD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   250 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmAQKEDMEERITTLEKRY 329
Cdd:pfam02029   91 PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA-EEEGEEEEDKSEEAEEV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   330 LSAQRESTSIHDMNDKLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRKAETLPEV---EAELAQRIAALTK 404
Cdd:pfam02029  170 PTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLEAEQK 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   405 AEErhgnieERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLsdtvdrlltesnerlqlhlKERMAALEEKNVLIQESE 484
Cdd:pfam02029  250 LEE------LRRRRQEKESEEFEKLRQKQQEAELELEELKKKR-------------------EERRKLLEEEEQRRKQEE 304
                          330       340
                   ....*....|....*....|....*.
gi 333805616   485 TFRKNLEESlhDKERLAEEIEKLRSE 510
Cdd:pfam02029  305 AERKLREEE--EKRRMKEEIERRRAE 328
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
241-424 2.22e-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: 41.59  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  241 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 311
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  312 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 389
Cdd:cd22656   152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 333805616  390 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 424
Cdd:cd22656   229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
PRK12704 PRK12704
phosphodiesterase; Provisional
365-513 2.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  365 RQLQERLELAEQKLQQTMRKAETlpevEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQELQRARQREKMNEEHn 444
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805616  445 krlsdtvdrlltesnerlqlhLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 513
Cdd:PRK12704   98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1012-1067 2.90e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.25  E-value: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616  1012 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1067
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
344-511 2.91e-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: 40.43  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   344 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 412
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEKQAEALEtqlaqqrsaveQL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   413 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 485
Cdd:pfam04012  117 RKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELA- 187
                          170       180
                   ....*....|....*....|....*.
gi 333805616   486 FRKNLEESLHDKERLAEEIEKLRSEL 511
Cdd:pfam04012  188 SAVDLDAKLEQAGIQMEVSEDVLARL 213
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
140-363 3.14e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   140 KRQAQSPSGVSSEvEVLKALKSLFEHhKALDEK----VRERLRVSLERVSALE--EELAAAN-QEIVALREQNVHIQRKM 212
Cdd:pfam05622  189 KRQVQELHGKLSE-ESKKADKLEFEY-KKLEEKlealQKEKERLIIERDTLREtnEELRCAQlQQAELSQADALLSPSSD 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   213 ASSEGSTESEHLEGMEPGQKV-HE-KRLSNGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETA 290
Cdd:pfam05622  267 PGDNLAAEIMPAEIREKLIRLqHEnKMLRLGQEGSYRE--RLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   291 RK----------DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylsaQRESTSIHDMNDKLENELANKEAILRQM 360
Cdd:pfam05622  345 QKalqeqgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELE------PKQDSNLAQKIDELQEALRKKDEDMKAM 418

                   ...
gi 333805616   361 EEK 363
Cdd:pfam05622  419 EER 421
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
357-470 3.36e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  357 LRQMEEKNRQLQ-ERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQ 435
Cdd:COG0542   413 LDELERRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616  436 R----EKMNEEHNKRLSDTVD-----------------RLLTESNERLqLHLKERM 470
Cdd:COG0542   493 ElaelEEELAELAPLLREEVTeediaevvsrwtgipvgKLLEGEREKL-LNLEEEL 547
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
256-434 3.75e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  256 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 335
Cdd:cd00176    64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  336 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 415
Cdd:cd00176   132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
                         170
                  ....*....|....*....
gi 333805616  416 MRHLEGQLEEKNQELQRAR 434
Cdd:cd00176   195 WEELLELAEERQKKLEEAL 213
PRK12704 PRK12704
phosphodiesterase; Provisional
285-442 4.07e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  285 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 364
Cdd:PRK12704   34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  365 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 432
Cdd:PRK12704   92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
                         170
                  ....*....|..
gi 333805616  433 ARQR--EKMNEE 442
Cdd:PRK12704  155 AKEIllEKVEEE 166
Caldesmon pfam02029
Caldesmon;
169-471 4.07e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   169 LDEKVRERLRVSLERVSALEEELAAANqEIVALREQNVHIQRKmassEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDE 248
Cdd:pfam02029   71 REERRQKRLQEALERQKEFDPTIADEK-ESVAERKENNEEEEN----SSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   249 TSQIVELQELLEKQNYEMAQMKERLAAlssRVGEVEQEAETARKDLIKTEEMNTKYQRD---IREAMAQKEDMEERITTL 325
Cdd:pfam02029  146 STEVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVT 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   326 EKRYLSAQRESTSIH-DMNDKLENELAnkeailrqMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveAELaqriaaltk 404
Cdd:pfam02029  223 TKRRQGGLSQSQEREeEAEVFLEAEQK--------LEELRRRRQEKESEEFEKLRQKQQEAE------LEL--------- 279
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805616   405 aEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA 471
Cdd:pfam02029  280 -EELKKKREERRKLLE---EEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
259-450 4.53e-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: 40.27  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  259 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 334
Cdd:cd07666    14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  335 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 399
Cdd:cd07666    93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805616  400 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 450
Cdd:cd07666   170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
251-462 5.04e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   251 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 330
Cdd:pfam01576  890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   331 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 409
Cdd:pfam01576  964 --------------KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRHADQYKDQAEK 1027
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333805616   410 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 462
Cdd:pfam01576 1028 GNS--RMKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESNESM 1070
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
160-449 6.13e-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: 40.90  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   160 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMASSEGSTESEHLEGMEPGQKVHEKR 237
Cdd:pfam09731  121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   238 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAE-TARKDLIKTEEM---------------- 300
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELvsifpdiipvlkednl 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   301 --NTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 377
Cdd:pfam09731  280 lsNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805616   378 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 449
Cdd:pfam09731  358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
RNase_Y_N pfam12072
RNase Y N-terminal region;
365-505 6.40e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   365 RQLQERLELAEQKLQQTMRKAETLP----------------EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 428
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   429 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 505
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
888-945 6.46e-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: 36.06  E-value: 6.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 333805616  888 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 945
Cdd:cd09487     2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
254-447 7.09e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   254 ELQELLEKQNYEMAQMKERLAALSSRvgEVEQEAETARKDLIKTEEmntKYQRDIRE-AMAQKEDMEERITTLEKRYLSA 332
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLQQSQ--EQWQAEKEQRKARLGREE---RRRADRREkQVIEKESRWREQAEDQENQRQE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   333 QRESTSIHDMNDKLENE--LANKEAILRQMEEKNR-QLQERLELAEQKLQQ--------------------TMRKAETLP 389
Cdd:pfam15558  110 KLERARQEAEQRKQCQEqrLKEKEEELQALREQNSlQLQERLEEACHKRQLkereeqkkvqennlsellnhQARKVLVDC 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805616   390 EVEAELAQRIAAL----TKAEERH-GNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRL 447
Cdd:pfam15558  190 QAKAEELLRRLSLeqslQRSQENYeQLVEERHRELREKAQKEEEQFQRAKWRaEEKEEERQEHK 253
46 PHA02562
endonuclease subunit; Provisional
194-409 8.16e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  194 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 261
Cdd:PHA02562  179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  262 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 332
Cdd:PHA02562  253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805616  333 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 409
Cdd:PHA02562  333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
354-523 8.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  354 EAILRQMEEKNRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 433
Cdd:PRK03918  138 DAILESDESREKVVRQILGLDDYE-----NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  434 RQREKmneehnkRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErlaEEIEKLRSELDQ 513
Cdd:PRK03918  213 SSELP-------ELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE---ERIEELKKEIEE 277
                         170
                  ....*....|
gi 333805616  514 LKMRTGSLIE 523
Cdd:PRK03918  278 LEEKVKELKE 287
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
43-403 8.94e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   43 DRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQEFAALTKELNACREQLLEKEEEISElKAERNNTRLLLEH 122
Cdd:COG5185   235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAE-YTKSIDIKKATES 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  123 LECLVSRHERSLRMTVVKRQAQSPSGVSSEvEVLKALKSLFEHHKALDEKVRERlrVSLERVSALEEELAAANQEIVALR 202
Cdd:COG5185   314 LEEQLAAAEAEQELEESKRETETGIQNLTA-EIEQGQESLTENLEAIKEEIENI--VGEVELSKSSEELDSFKDTIESTK 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  203 EQNVHIQRKMASSegstESEHLEGMEPGQKVHEKrlsngsidstdetsQIVELQELLEKQNYEMAQMKERLAALSSRVGE 282
Cdd:COG5185   391 ESLDEIPQNQRGY----AQEILATLEDTLKAADR--------------QIEELQRQIEQATSSNEEVSKLLNELISELNK 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  283 VEQEAetarkDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEE 362
Cdd:COG5185   453 VMREA-----DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAE 524
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 333805616  363 K-NRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALT 403
Cdd:COG5185   525 SlKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLR 566
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
374-515 8.98e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 8.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616   374 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 449
Cdd:pfam02841  174 AEEVLQEFLQSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805616   450 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 515
Cdd:pfam02841  251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
1012-1056 9.03e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 9.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 333805616 1012 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1056
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
46 PHA02562
endonuclease subunit; Provisional
276-515 9.94e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  276 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 352
Cdd:PHA02562  172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  353 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 430
Cdd:PHA02562  246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805616  431 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 510
Cdd:PHA02562  323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387

                  ....*
gi 333805616  511 LDQLK 515
Cdd:PHA02562  388 LDKIV 392
 
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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