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Conserved domains on  [gi|333805618|ref|NP_001207405|]
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liprin-alpha-2 isoform e [Homo sapiens]

Protein Classification

liprin-alpha( domain architecture ID 13377566)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
1098-1169 3.68e-44

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


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.68e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
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 ...
895-965 6.55e-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: 6.55e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618  895 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 965
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 ...
1013-1078 1.14e-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: 1.14e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 1013 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1078
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-533 5.41e-18

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 90.16  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  201 RVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQ 280
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLE-----DLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  281 NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 360
Cdd:COG1196   743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  361 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ 440
Cdd:COG1196   823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  441 LEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-------NVL-IQESETFRKNLEES 511
Cdd:COG1196   903 LKEEIEKLrERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEiealgpvNLRaIEEYEEVEERYEEL 982
                         330       340
                  ....*....|....*....|..
gi 333805618  512 LHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196   983 KSQREDLEEAKEKLLEVIEELD 1004
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-329 2.32e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.02  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGLAgskgadppefaALTKELNACREQLL 118
Cdd:COG1196   736 QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK-LKEEIEELEEKRQ-----------ALQEELEELEEELE 803
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  119 EKEEEISELKAERNNTRLLLEHLEclVSRHERSLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRERLRV 197
Cdd:COG1196   804 EAERRLDALERELESLEQRRERLE--QEIEELEEEIEELEEKLDELEEELEELEkELEELKEELEELEAEKEELEDELKE 881
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  198 SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELL 277
Cdd:COG1196   882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEAL 961
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618  278 EKQNY----EMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREA 329
Cdd:COG1196   962 GPVNLraieEYEEVEERYEELKSQREDLEEAKEKLLE---VIEELDKEKRERFKET 1014
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
1098-1169 3.68e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.68e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
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 ...
895-965 6.55e-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: 6.55e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618  895 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 965
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 ...
1013-1078 1.14e-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: 1.14e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 1013 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1078
Cdd:cd09565     1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-533 5.41e-18

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 90.16  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  201 RVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQ 280
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLE-----DLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  281 NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 360
Cdd:COG1196   743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  361 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ 440
Cdd:COG1196   823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  441 LEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-------NVL-IQESETFRKNLEES 511
Cdd:COG1196   903 LKEEIEKLrERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEiealgpvNLRaIEEYEEVEERYEEL 982
                         330       340
                  ....*....|....*....|..
gi 333805618  512 LHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196   983 KSQREDLEEAKEKLLEVIEELD 1004
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
83-481 6.33e-16

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 83.57  E-value: 6.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    83 QDIESLTGGLAGSKGADPPEFAAL--TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ 160
Cdd:TIGR02168  650 LDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   161 AQSPSGVSSEVEVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESE 240
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   241 HLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT 320
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   321 KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQT 399
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEA 956
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   400 MRKAETLPEVEAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNK 463
Cdd:TIGR02168  957 EALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARE 1032
                          410
                   ....*....|....*...
gi 333805618   464 RLSDTVDRLltesNERLQ 481
Cdd:TIGR02168 1033 RFKDTFDQV----NENFQ 1046
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-589 1.27e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 78.93  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 261
Cdd:PRK02224  264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  262 DSTDETSQIVELqellekqnyemaqmKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 341
Cdd:PRK02224  336 AAQAHNEEAESL--------------REDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 419
Cdd:PRK02224  395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 496
Cdd:PRK02224  470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  497 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 576
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
                         490
                  ....*....|...
gi 333805618  577 RPRRGRMGVRRDE 589
Cdd:PRK02224  626 RERLAEKRERKRE 638
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1012-1076 6.90e-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 heterooligomerize with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 67.29  E-value: 6.90e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  1012 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
265-530 2.81e-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 characteristic 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: 63.93  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 424
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   425 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 490
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 333805618   491 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 530
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
895-961 5.73e-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: 5.73e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618    895 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 961
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1021-1076 1.18e-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: 1.18e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618   1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1099-1170 7.15e-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: 7.15e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618   1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1170
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-329 2.32e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.02  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGLAgskgadppefaALTKELNACREQLL 118
Cdd:COG1196   736 QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK-LKEEIEELEEKRQ-----------ALQEELEELEEELE 803
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  119 EKEEEISELKAERNNTRLLLEHLEclVSRHERSLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRERLRV 197
Cdd:COG1196   804 EAERRLDALERELESLEQRRERLE--QEIEELEEEIEELEEKLDELEEELEELEkELEELKEELEELEAEKEELEDELKE 881
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  198 SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELL 277
Cdd:COG1196   882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEAL 961
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618  278 EKQNY----EMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREA 329
Cdd:COG1196   962 GPVNLraieEYEEVEERYEELKSQREDLEEAKEKLLE---VIEELDKEKRERFKET 1014
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
897-961 1.26e-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 heterooligomerize with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618   897 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 961
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1099-1169 1.48e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618  1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1169
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
362-536 6.73e-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: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  362 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 429
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  430 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 499
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 333805618  500 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 536
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 ...
1098-1169 3.68e-44

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 154.01  E-value: 3.68e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
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 ...
895-965 6.55e-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: 6.55e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618  895 FAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 965
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 ...
1013-1078 1.14e-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: 1.14e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618 1013 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 1078
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 ...
1017-1076 2.31e-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: 2.31e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618 1017 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
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 ...
902-960 3.85e-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: 3.85e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618  902 TVVAWLELWLGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 960
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 ...
1106-1167 7.51e-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: 7.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1106 RVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNN 1167
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 ...
1098-1169 1.46e-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: 1.46e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-533 5.41e-18

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 90.16  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  201 RVSALEEELAAANQEIVALREQNVHIQRKMASSEgstesEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQ 280
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLE-----DLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  281 NYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDM 360
Cdd:COG1196   743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQR 822
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  361 NDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ 440
Cdd:COG1196   823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAE 902
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  441 LEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK-------NVL-IQESETFRKNLEES 511
Cdd:COG1196   903 LKEEIEKLrERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEiealgpvNLRaIEEYEEVEERYEEL 982
                         330       340
                  ....*....|....*....|..
gi 333805618  512 LHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196   983 KSQREDLEEAKEKLLEVIEELD 1004
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
87-471 4.83e-17

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 87.08  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   87 SLTGGLAGSKG--ADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqaqsp 164
Cdd:COG1196   651 SITGGSRNKRSslAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEE---------- 720
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  165 sgvssevevlkaLKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEG 244
Cdd:COG1196   721 ------------LKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLK--EEIEELEE 786
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  245 MEPGQKVHEKRLsNGSIDSTDEtsQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR 324
Cdd:COG1196   787 KRQALQEELEEL-EEELEEAER--RLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  325 DIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAE 404
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEE-YEDT 942
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  405 TLPEVEAELAQ---RIAAL----TKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDR 471
Cdd:COG1196   943 LETELEREIERleeEIEALgpvnLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEViEELDKEKRERFKETFDK 1017
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
896-960 6.27e-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: 6.27e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  896 AQWDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 960
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 ...
1012-1076 1.83e-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: 1.83e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 1012 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
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 ...
1012-1076 1.89e-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: 1.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618 1012 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
83-481 6.33e-16

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 83.57  E-value: 6.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    83 QDIESLTGGLAGSKGADPPEFAAL--TKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQ 160
Cdd:TIGR02168  650 LDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   161 AQSPSGVSSEVEVLKALKSLFEHHKALDEkVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRkmASSEGSTESE 240
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ--LKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   241 HLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNT 320
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   321 KYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERL-ELAEQKLQQT 399
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEA 956
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   400 MRKAETLPEVEAELAQRIAALTKAEERHGNI-----------EERMRHLEGQLEeknqELQRARQR-----EKMNEEHNK 463
Cdd:TIGR02168  957 EALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARE 1032
                          410
                   ....*....|....*...
gi 333805618   464 RLSDTVDRLltesNERLQ 481
Cdd:TIGR02168 1033 RFKDTFDQV----NENFQ 1046
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
269-539 6.65e-16

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 83.23  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYl 348
Cdd:COG1196   233 KLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERL- 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  349 saqrestsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH- 427
Cdd:COG1196   312 -------------EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELf 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  428 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTE------SNERLQLHLKERMAALEEKNVLIQES 501
Cdd:COG1196   379 EALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEElkeleaELEELQTELEELNEELEELEEQLEEL 458
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 333805618  502 ETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:COG1196   459 RDRLKELEREL---AELQEELQRLEKELSSLEARLDRL 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-529 1.87e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 82.03  E-value: 1.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQdIESLTGGLAGSKGadppEFAALTKELNACREQLLE 119
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEA----ELEELESRLEELEEQLET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEvevLKALKSLFEHHKALDEKVRERLRVSL 199
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   200 ERVSALEEELAAANQEIVALREQNVHIQRKMASSEgsTESEHLEGMEPGQK--VHEKRLSNG---------SIDSTDET- 267
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--RLQENLEGFSEGVKalLKNQSGLSGilgvlseliSVDEGYEAa 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   268 -----------------SQIVELQELLEKQNYEMAQMKE----RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQR-- 324
Cdd:TIGR02168  539 ieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKal 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   325 -----------DIREAMAQ--KEDMEERITTLE-----KRYLSAQRESTSIHDMNDKlENELANKEAILRQMEEKNRQLQ 386
Cdd:TIGR02168  619 syllggvlvvdDLDNALELakKLRPGYRIVTLDgdlvrPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIAELE 697
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   387 ERLELAEQKLQQTMRKAETLPEVEAELAQRIAA----LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN 462
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618   463 KRLSD---TVDRLLTESNERLQLhLKERMAALEEK----NVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:TIGR02168  778 AEAEAeieELEAQIEQLKEELKA-LREALDELRAEltllNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
1098-1169 2.53e-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: 2.53e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1098 DVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLL 1169
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-534 3.22e-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: 3.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   347 YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   427 hgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERL-QLHLKERMAALEEKNVLIQESE 502
Cdd:TIGR02168  871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrreLEELREKLaQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270
                   ....*....|....*....|....*....|..
gi 333805618   503 TFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
288-541 4.72e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.49  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   288 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENE 367
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   368 LANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRIAALTKAEERH-------GNIEERMRHLEGQ 440
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   441 LEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLHLKER-------MAALEEKNVLIQESETFRKNLEE 510
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERasleealALLRSELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|.
gi 333805618   511 SLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQE 943
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
283-535 6.62e-15

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.14  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  283 EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMND 362
Cdd:COG1196   668 ELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELE 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  363 KLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 442
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEEL---EEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  443 EKNQELQRARQREKMNEEHNKRLSDTVDRLlTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESL----HDKERL 518
Cdd:COG1196   825 RLEQEIEELEEEIEELEEKLDELEEELEEL-EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELreleSELAEL 903
                         250
                  ....*....|....*..
gi 333805618  519 AEEIEKLRSELDQLKMR 535
Cdd:COG1196   904 KEEIEKLRERLEELEAK 920
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
263-535 6.68e-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: 6.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   263 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITT 342
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   343 LEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   423 AEERHGNIEERMRHLEGQLEEKNQELQRAR-QREKMNEEHNKrlsdtVDRLLTESNERLQLHLKERMAALEEKNVLIQES 501
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270
                   ....*....|....*....|....*....|....
gi 333805618   502 ETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR 930
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
265-535 7.91e-15

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 79.76  E-value: 7.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQ-------EAETARKDLIKTEEM----NTKYQRDIREAMAQK 333
Cdd:COG1196   162 EEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKqleklerQAEKAERYQELKAELreleLALLLAKLKELRKEL 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  334 EDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG1196   242 EELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEEL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  414 AQRIAALtkaEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEE 493
Cdd:COG1196   322 EERLEEL---KEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNE 398
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 333805618  494 KNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG1196   399 LEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTE 440
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
231-534 1.14e-14

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 79.37  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  231 ASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK 310
Cdd:COG1196   665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  311 DLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLE 390
Cdd:COG1196   745 ELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  391 LAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErhgNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVD 470
Cdd:COG1196   825 RLEQEIEELEEEIEELEEKLDELEEELEELEKELE---ELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618  471 RLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErLAEEIEKLRSELDQLKM 534
Cdd:COG1196   902 ELKEE-IEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETE-LEREIERLEEEIEALGP 963
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
174-527 1.23e-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: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   174 LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE 253
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   254 KRlsngsidstdetSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK 333
Cdd:TIGR02168  780 AE------------AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   334 EDMEERITTLEKRYLSAQREStsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAEL 413
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELR----------ELESKR 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   414 AQRIAALTKAEERHGNIEERMRHLEGQLEEKnqeLQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMAALEE 493
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 333805618   494 KNVL-IQESETFRKNLEESLHDKERLAEEIEKLRS 527
Cdd:TIGR02168  987 VNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-589 1.27e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 78.93  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLrmtvvkrqaqspsgvsSEVEVLKALKSLF 181
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----------------EELETLEAEIEDL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREqnvhiqrkMASSEGSTESEHLEGMEPGQKVHEKRLSNGSI 261
Cdd:PRK02224  264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEELRDRLEECRV 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  262 DSTDETSQIVELqellekqnyemaqmKERLAALSSRVGEVEQEAETARKDLIKTEEmntkyqrDIREAMAQKEDMEERIT 341
Cdd:PRK02224  336 AAQAHNEEAESL--------------REDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIE 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  342 TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQklqqtMRKAETLPEVEAEL--AQRIAA 419
Cdd:PRK02224  395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVegSPHVET 469
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLS--DTVDRLLTESNERLQlHLKERMAAL-EEKNV 496
Cdd:PRK02224  470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAE 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  497 LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLiePTIpRTHLDTSAELRYSVGSLVDSQSDYRTTKVIR 576
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERI-RTLLAAIADAEDEIERLREKREALAELNDER 625
                         490
                  ....*....|...
gi 333805618  577 RPRRGRMGVRRDE 589
Cdd:PRK02224  626 RERLAEKRERKRE 638
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
114-533 2.50e-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: 78.19  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   114 REQLLEKEEEISELKAERNNTRLLLEHLECLVsrHERSLRMTVVKRQAqspSGVSSEVEVLKAlkslfEHhkaldEKVRE 193
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRL--DELSQELSDASRKI---GEIEKEIEQLEQ-----EE-----EKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   194 RLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMAssegstesehlegmepgqKVHEKRLSNGSIDSTDETSQIVEL 273
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEAR---IEELEE------------------DLHKLEEALNDLEARLSHSRIPEI 796
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   274 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARkdliktEEMNTKyQRDIREAMAQKEDMEERITTLEKRYlsaqre 353
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE------KEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK------ 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   354 stsihdmnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpEVEAELAQRIAALTKAeeRHGNIEER 433
Cdd:TIGR02169  864 --------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA--KLEALEEE 932
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   434 MRHLE---GQLEEKNQELQRARQREKMNEEhnkrlsdtvdrlltesnerlqlhLKERMAALEEKNVL-IQESETFRKNLE 509
Cdd:TIGR02169  933 LSEIEdpkGEDEEIPEEELSLEDVQAELQR-----------------------VEEEIRALEPVNMLaIQEYEEVLKRLD 989
                          410       420
                   ....*....|....*....|....*..
gi 333805618   510 ESLHDKERLAEE---IEKLRSELDQLK 533
Cdd:TIGR02169  990 ELKEKRAKLEEErkaILERIEEYEKKK 1016
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
1012-1076 6.90e-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 heterooligomerize with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 67.29  E-value: 6.90e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  1012 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
41-697 1.79e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 75.52  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGglagskgadppEFAALTKELNACREQLLEK 120
Cdd:COG1196   226 ELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAE-KEIEELKS-----------ELEELREELEELQEELLEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  121 EEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLE 200
Cdd:COG1196   294 KEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALK-EELEERETLLEELEQLLAELEEAKEELEEKLSALLE 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  201 ----RVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQ 274
Cdd:COG1196   373 eleeLFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEElnEELEELE 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  275 ELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTL------EKRYL 348
Cdd:COG1196   453 EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVaelikvKEKYE 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  349 SA--------------------------------------------QRESTSIHDMNDKL-----------ENELANKeA 373
Cdd:COG1196   533 TAleaalgnrlqavvveneevakkaieflkenkagratflpldrikPLRSLKSDAAPGFLglasdlidfdpKYEPAVR-F 611
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  374 ILRQ-----MEEKNRQLQERLEL---------------------AEQKLQQTMRKAEtLPEVEAELAQRIAALTKAEERH 427
Cdd:COG1196   612 VLGDtlvvdDLEQARRLARKLRIkyrivtldgdlvepsgsitggSRNKRSSLAQKRE-LKELEEELAELEAQLEKLEEEL 690
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  428 GNIEERMRHLEGQLEEKNQELQRARqrekMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKN 507
Cdd:COG1196   691 KSLKNELRSLEDLLEELRRQLEELE----RQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEE 766
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEptiprthldTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRR 587
Cdd:COG1196   767 LESLEEALAKLKEEIEELEEKRQALQEELEELEE---------ELEEAERRLDALERELESLEQRRERLEQEIEELEEEI 837
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  588 DE--PKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDdretifssmdllspsgHSDAQTLAMMLQEQLDAINKEIR 665
Cdd:COG1196   838 EEleEKLDELEEELEELEKELEELKEELEELEAEKEELEDE----------------LKELEEEKEELEEELRELESELA 901
                         730       740       750
                  ....*....|....*....|....*....|..
gi 333805618  666 LIQEEKESTELRAEEIENRVASVSLEGLNLAR 697
Cdd:COG1196   902 ELKEEIEKLRERLEELEAKLERLEVELPELEE 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
290-533 2.31e-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: 2.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   290 RLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELA 369
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   370 NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI----AALTKAEERHGNIEERMRHLEGQLEEKN 445
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   446 QELQRARQREKMNEEHNKRLSDTVDRlLTESNERLQLHLKERMAALEEKNV--LIQESETFRKNLEESLHDKERLAEEIE 523
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALE 464
                          250
                   ....*....|
gi 333805618   524 KLRSELDQLK 533
Cdd:TIGR02168  465 ELREELEEAE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-539 3.41e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 74.71  E-value: 3.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   349 SAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRIAALTKAEERHG 428
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   429 NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE-EKNVLIQESETFRKN 507
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEA 462
                          250       260       270
                   ....*....|....*....|....*....|..
gi 333805618   508 LEESLHDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
115-443 4.51e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.98  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVR-- 192
Cdd:COG1196   179 RKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEel 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTD 265
Cdd:COG1196   259 qEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISllrerlEELENELEELEERLEELKEKIEALKEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 345
Cdd:COG1196   339 LEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSE 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  346 RYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE 425
Cdd:COG1196   419 RLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQR 498
                         330
                  ....*....|....*...
gi 333805618  426 RHGNIEERMRHLEGQLEE 443
Cdd:COG1196   499 ASQGVRAVLEALESGLPG 516
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
114-478 5.62e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.98  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  114 REQLLEKEEEISELKAERNNTRLLLEHLEclvsrhERSLRMTVVKRQaqspsgVSSEVEVLKALKSLFEHHKALDEKVRE 193
Cdd:COG1196   157 RRKLIEEAAGVSKYKERKEEAERKLERTE------ENLERLEDLLEE------LEKQLEKLERQAEKAERYQELKAELRE 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  194 -RLRVSLERVSALEEELAAANQEIVALREQnvHIQRKMASSEGSTESEHLEgmepgQKVHEKRLsngsiDSTDETSQIVE 272
Cdd:COG1196   225 lELALLLAKLKELRKELEELEEELSRLEEE--LEELQEELEEAEKEIEELK-----SELEELRE-----ELEELQEELLE 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-KRYLSAQ 351
Cdd:COG1196   293 LKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEeKLSALLE 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  352 RESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE 431
Cdd:COG1196   373 ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELE 452
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 333805618  432 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNE 478
Cdd:COG1196   453 EQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRA 499
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
31-533 8.71e-13

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 72.87  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   31 FEQLMVNMLDERDRLLDTLRETQEsLSLAQQRLQDVIYD----RDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAAL 106
Cdd:COG0419   145 FDAFLKSKPKERKEILDELFGLEK-YEKLSELLKEVIKEakakIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  107 TKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrHERSLRMTVVKRQAQSpsgvssEVEVLKALKSLFEHHKA 186
Cdd:COG0419   224 EQEEEELEQEIEALEERLAELEEEKERLEELKARLL-----EIESLELEALKIREEE------LRELERLLEELEEKIER 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  187 LDEKVRE--RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKM--ASSEGSTESEHLEGMEPGQKVHEKRLSNGSID 262
Cdd:COG0419   293 LEELEREieELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLekLESELEELAEEKNELAKLLEERLKELEERLEE 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  263 STDETSQIVELQELLEKQnyeMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITT 342
Cdd:COG0419   373 LEKELEKALERLKQLEEA---IQELKEELAELSAALEEIQEELEELEKEL-------EELERELEELEEEIKKLEEQINQ 442
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  343 LEKRYLSAqRESTSIHDMNDKLENELANkeailrqmeEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 422
Cdd:COG0419   443 LESKELMI-AELAGAGEKCPVCGQELPE---------EHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRE 512
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  423 AEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdRLLTESNERLQLHLKERMAALEEknvliqese 502
Cdd:COG0419   513 LEEELIELLELEEALKEELEEKLEKLENLLEELEELKE----------KLQLQQLKEELRQLEDRLQELKE--------- 573
                         490       500       510
                  ....*....|....*....|....*....|.
gi 333805618  503 tfrknLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG0419   574 -----LLEELRLLRTRKEELEELRERLKELK 599
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
895-959 1.65e-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: 1.65e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618  895 FAQWDGPTVVAWL-ELWLGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 959
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
32-541 1.86e-12

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 72.10  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   32 EQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALpQDIESLTGGLAGSKGADPPEFAALTKELN 111
Cdd:COG0419   192 GQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERL-AELEEEKERLEELKARLLEIESLELEALK 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  112 ACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHER-----SLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKA 186
Cdd:COG0419   271 IREEELRELERLLEELEEKIERLEELEREIEELEEELEGlrallEELEELLEKLKSLEERLEKLEEKLEKLESELEELAE 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  187 LDEKVRERLRvslERVSALEEELAAANQEIVALRE--QNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSngsiDST 264
Cdd:COG0419   351 EKNELAKLLE---ERLKELEERLEELEKELEKALErlKQLEEAIQELKEELAELSAALEEIQEELEELEKELE----ELE 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVG-------EVEQEAETARKDLIKTEEMNTKYQRDIREamaQKEDME 337
Cdd:COG0419   424 RELEELEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcgqELPEEHEKELLELYELELEELEEELSREK---EEAELR 500
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  338 ERITTLEKRYLSAQRESTSIHDMNDKLENEL-ANKEAILRQMEE----KNRQLQERLELAEQKLQQTMRKAETLPEVEAE 412
Cdd:COG0419   501 EEIEELEKELRELEEELIELLELEEALKEELeEKLEKLENLLEEleelKEKLQLQQLKEELRQLEDRLQELKELLEELRL 580
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  413 LAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHN--KRLSDTVDRL-----LTESNERLQLHLK 485
Cdd:COG0419   581 LRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEaeEELESELEKLnlqaeLEELLQAALEELE 660
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618  486 ERMAALEEK-NVLIQESETfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG0419   661 EKVEELEAEiRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQ 716
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
40-533 2.91e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 71.28  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   40 DERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNsalpqDIESLTGGLAGSKGADPPEFAALTKELNACREQLLE 119
Cdd:COG1196   383 EELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKEELKELEAELEELQTELEELNEELEELEEQLEE 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  120 KEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSPSGVSsevEVLKALKSLFEHHKALdekVRERLRVSL 199
Cdd:COG1196   458 LRDRLKELERELAELQEELQRLEKELSSLEARLDRL--EAEQRASQGVR---AVLEALESGLPGVYGP---VAELIKVKE 529
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  200 ERVSALEEELAAANQEIVALREQ-NVHIQRKMASSEGSTESE-HLEGMEPGqKVHEKRLSNGSIDSTdetSQIVELQELL 277
Cdd:COG1196   530 KYETALEAALGNRLQAVVVENEEvAKKAIEFLKENKAGRATFlPLDRIKPL-RSLKSDAAPGFLGLA---SDLIDFDPKY 605
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  278 EKQNY----------EMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemNTKYQRDIREAMAQKEDMEERITTLEKRY 347
Cdd:COG1196   606 EPAVRfvlgdtlvvdDLEQARRLARKLRIKYRIVTLDGDLVEPSGSITG--GSRNKRSSLAQKRELKELEEELAELEAQL 683
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  348 LSAQRESTSIHDMNDKLENELANKEAILRQM--------------EEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG1196   684 EKLEEELKSLKNELRSLEDLLEELRRQLEELerqleelkrelaalEEELEQLQSRLEELEEELEELEEELEELQERLEEL 763
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  414 AQRIAALTKA----EERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQ--LHLKER 487
Cdd:COG1196   764 EEELESLEEAlaklKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEeiEELEEK 843
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 333805618  488 MAALEEKNVLIQES-ETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1196   844 LDELEEELEELEKElEELKEELEELEAEKEELEDELKELEEEKEELE 890
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
108-534 2.99e-12

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 71.33  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKAL 187
Cdd:COG0419   322 EKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKE----LEKALERLKQLEEAIQELKEE 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  188 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQR-KMASSEGSTESEHLEGME--------PGQKVHEKRLS- 257
Cdd:COG0419   398 LAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEqINQLESKELMIAELAGAGekcpvcgqELPEEHEKELLe 477
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  258 ---------NGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSS-RVGEVEQEAETARKDLIKTEEMNTKYQR-DI 326
Cdd:COG0419   478 lyeleleelEEELSREKEEAELREEIEELEKELRELEEELIELLELEEaLKEELEEKLEKLENLLEELEELKEKLQLqQL 557
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  327 REAMAQKEDMEERITTLEKRYLsaqrestsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL 406
Cdd:COG0419   558 KEELRQLEDRLQELKELLEELR---------------LLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELS 622
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  407 pEVEAELAQRIAALTKAEERHG-------NIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTvdrlltesnER 479
Cdd:COG0419   623 -EAENELEEAEEELESELEKLNlqaeleeLLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEEL---------EQ 692
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  480 LQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKM 534
Cdd:COG0419   693 LEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALELLEE 747
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
255-539 4.95e-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: 4.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   255 RLSNGSIDSTDETSQIVELQELLEKqnyemaqMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE 334
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   335 DMEERITTLEKRYLSAQRESTSIHDMNDKLENELAnkeailrQMEEKNRQLQERLELAEQKLQQtmrkaETLPEVEAEla 414
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSH-----SRIPEIQAE-- 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   415 qriaaLTKAEERHGNIEERMRHLEGQLEEKNQELQRArqREKMNEEHNKRlsdtvdRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR02169  800 -----LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQR------IDLKEQIKSIEKEIENLNGKKEEL 866
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 333805618   495 NVLIQESETFRKNLEESLHDkerLAEEIEKLRSELDQLKMRTGSL 539
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEEL 908
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
169-460 8.50e-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: 8.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   169 SEVEVLKALKSLFEHHKALDEKVRERLrvslERVSALEEELAAANQEIVAL-REQNVHIQRKMASSEGSTES--EHLEGM 245
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASleRSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   246 EPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRD 325
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   326 IREAmaqKEDMEERITTLEKRYLSAQRESTSIHDMNdkleNELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaet 405
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL------ 460
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 333805618   406 lpeveaelaqrIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:TIGR02169  461 -----------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-541 8.83e-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: 8.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   265 DETSQIVELQELLEKQNYEMAQMKERLA-------ALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   338 ERITTLEKRYLSAQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpevEAELAQRI 417
Cdd:TIGR02168  337 EELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLE 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRAR--QREKMNEEHNKRLSDTVDRLLTESNERLQlhLKERMAALEEKN 495
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEE--AEQALDAAEREL 484
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 333805618   496 VLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-535 6.16e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.01  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918  232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEEY 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLSNGS 260
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLT 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  261 IDSTDETSQIV-----ELQELLEKQNYEMAQMKERLAALSSRVGEVEQE-----------AETARKDLIK--TEEMNtKY 322
Cdd:PRK03918  386 PEKLEKELEELekakeEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLEeyTAELK-RI 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  323 QRDIREAMAQKEDMEERITTLEKrYLSAQRESTSIHDMNDKLEN-ELANKEAILRQMEEKNRQ---LQERLELAEQKLQQ 398
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKS 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  399 TMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHL----EGQLEEKNQELqrarqrEKMNEEHNkRLSDTVDRL-- 472
Cdd:PRK03918  544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKEL------EPFYNEYL-ELKDAEKELer 616
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618  473 LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKE---------RLAEEIEKLRSELDQLKMR 535
Cdd:PRK03918  617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELAGLRAELEELEKR 688
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-427 7.09e-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: 67.00  E-value: 7.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    49 LRETQESLslaqQRLQDVIYDR----DSLQRQLNSA-----------------LPQDIESLTGGLAGSKGadppEFAALT 107
Cdd:TIGR02168  181 LERTRENL----DRLEDILNELerqlKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQE----ELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   108 KELNACREQLLEKEEEISELKAERNNTRLLLEHLEclvsrherslrmtvvkrqaqspsgvsSEVEVLKALKSLFEHHKal 187
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQ--------------------------KELYALANEISRLEQQK-- 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   188 dekvrERLRVSLERvsaLEEELAAANQEIVALREQNVHIQRKMASSEgstesehlegmepgqkvhekrlsngsidstdet 267
Cdd:TIGR02168  305 -----QILRERLAN---LERQLEELEAQLEELESKLDELAEELAELE--------------------------------- 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   268 SQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRy 347
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE- 422
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   348 LSAQRESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERH 427
Cdd:TIGR02168  423 IEELLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-540 8.15e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  104 AALTKELNACREQL---LEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVvkrqaqspSGVSSEVEVLKALKSL 180
Cdd:PRK03918  168 GEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--------EKLEKEVKELEELKEE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  181 FEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNGS 260
Cdd:PRK03918  240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---VKELKELKEKAEEYIKLSEF---YEEYLDELREIE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  261 IDSTDETSQIVELQELLEKqnyemaqmkerLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRdIREAMAQKEDMEERI 340
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKE-----------LEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRL 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  341 T-----TLEKRYLSAQRESTSIHDMNDKLENELANkeaiLRQMEEKNRQLQERLELAEQKLQQTMR------KAETLPEV 409
Cdd:PRK03918  382 TgltpeKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRelteehRKELLEEY 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  410 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEeKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLhLKERMA 489
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLI 535
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805618  490 ALEEKnvliqesetfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:PRK03918  536 KLKGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
266-541 8.29e-11

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 66.71  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK--EDMEERITTL 343
Cdd:COG0419   165 GLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQeiEALEERLAEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  344 EKRYLSAQRESTSIHDMN-------DKLENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKAETLPEVEAEL 413
Cdd:COG0419   245 EEEKERLEELKARLLEIEslelealKIREEELRELERLLEELEEKIERLEElerEIEELEEELEGLRALLEELEELLEKL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  414 AQRIAALTKAEERHGNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTVDRLL------TESNERLQLHLKER 487
Cdd:COG0419   325 KSLEERLEKLEEKLEKLESELEELA---EEKNELAKLLEERLKELEERLEELEKELEKALerlkqlEEAIQELKEELAEL 401
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 333805618  488 MAALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG0419   402 SAALEEIQEELEELEKELEELEREL---EELEEEIKKLEEQINQLESKELMIAE 452
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
39-532 1.71e-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: 65.76  E-value: 1.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIE--SLTGGLAGSKGADPPEFAALTKELNACREQ 116
Cdd:TIGR00618  371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   117 LLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRM-TVVKRQAQSPSGVSSEVEvlKALKSLFEHHKALDEK--VRE 193
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPgpLTR 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   194 RLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTE------SEHLEGMEPGQKVHEKRLSNGSIDSTDET 267
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   268 SQIVELQELLEKQNYEMAqmKERLAALSSRVGEVEQEAETArkdliKTEEMNTKYQRDIREAMAQKEDMEERitTLEKRY 347
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTA-----LHALQLTLTQERVREHALSIRVLPKE--LLASRQ 679
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   348 LSAQRESTSIHDMNDKLEnELANKEAILRQMEE---KNRQLQERLELAEQKLQQTMR-KAETLPEVEAEL-AQRIAALTK 422
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKE-MLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKA 758
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   423 AEERHGNIEER----------MRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:TIGR00618  759 RTEAHFNNNEEvtaalqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 333805618   493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
265-530 2.81e-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 characteristic 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: 63.93  E-value: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE 344
Cdd:pfam19220   45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE 424
Cdd:pfam19220  125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   425 ERHgniEERMRHLEGQLEEKNQELQRA-RQREKMNEEHNKRLSD-------------TVDRLLTESNERLQlHLKERMAA 490
Cdd:pfam19220  205 DAT---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERASlrmklealtaraaATEQLLAEARNQLR-DRDEAIRA 280
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 333805618   491 LEEKNV-LIQESETFRKNLEESLHDKERLAE---EIEKLRSELD 530
Cdd:pfam19220  281 AERRLKeASIERDTLERRLAGLEADLERRTQqfqEMQRARAELE 324
PTZ00121 PTZ00121
MAEBL; Provisional
109-514 3.50e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  109 ELNACREQLLEKEEEISELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALD 188
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  189 E--KVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMAssEGSTESEHLEGMEPGQKVHEKRLSNgSIDSTDE 266
Cdd:PTZ00121 1474 EakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAE-EKKKADE 1550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMAQKEDMEERITTLEKR 346
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  347 ylSAQRESTSIHDMNDKLENEL--------ANKEAILRQMEEKNRQLQERLELAE-QKLQQTMRKAETLPEVEAELAQRI 417
Cdd:PTZ00121 1627 --KAEEEKKKVEQLKKKEAEEKkkaeelkkAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKA 1704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKR---LSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
                         410       420
                  ....*....|....*....|
gi 333805618  495 nvLIQESETFRKNLEESLHD 514
Cdd:PTZ00121 1785 --LDEEDEKRRMEVDKKIKD 1802
mukB PRK04863
chromosome partition protein MukB;
192-539 4.98e-10

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 64.21  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  192 RERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEts 268
Cdd:PRK04863  278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemntkyqrdireamaqkEDMEERITTLEKR-- 346
Cdd:PRK04863  356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL---------------------ADYQQALDVQQTRai 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  347 -YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRIAALTKAEE 425
Cdd:PRK04863  415 qYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSE 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  426 RHgnieERMRHLEGQLEEKNQELQRARQ-REKMNE-EHNKRLSDTVDRLLTESNERLQLHLkERMAALEEknvLIQESET 503
Cdd:PRK04863  494 AW----DVARELLRRLREQRHLAEQLQQlRMRLSElEQRLRQQQRAERLLAEFCKRLGKNL-DDEDELEQ---LQEELEA 565
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 333805618  504 FRKNLEESlhdKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK04863  566 RLESLSES---VSEARERRMALRQQLEQLQARIQRL 598
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-539 8.80e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  175 KALKSLFEHHKALDEKvRERLRVSLERVSALEEELAAANQEIvalrEQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEK 254
Cdd:PRK03918  162 NAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKEL----EEVLREINEISSELPELREE-LEKLEKEVKELEE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  255 RlsngsidstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE---QEAETARKDLIKTEEMNTKYQRDIR---E 328
Cdd:PRK03918  236 L-----------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIKLSEfyeE 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  329 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQME---------EKNRQLQERLELAEQKLqqt 399
Cdd:PRK03918  305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEELERLKKRL--- 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  400 mrKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ---ELQRARQR-----EKMNEEHNKRLSDTVDR 471
Cdd:PRK03918  382 --TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKcpvcgRELTEEHRKELLEEYTA 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  472 LLTESNERLQ-LHLKERMAALEEKNV---LIQESETFR--------KNLEESL--HDKERL---AEEIEKLRSELDQLKM 534
Cdd:PRK03918  460 ELKRIEKELKeIEEKERKLRKELRELekvLKKESELIKlkelaeqlKELEEKLkkYNLEELekkAEEYEKLKEKLIKLKG 539

                  ....*
gi 333805618  535 RTGSL 539
Cdd:PRK03918  540 EIKSL 544
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-533 1.18e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPSGVSSEV-EVLKALKSLFEHHKALDEKVR- 192
Cdd:PRK03918  286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHEl 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  193 -ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEpgQKVHEKRLSNGSIDSTDETSQIV 271
Cdd:PRK03918  364 yEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKAIEELKKAKGKCPVC 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  272 -------ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-----------------RDIR 327
Cdd:PRK03918  442 grelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkeleeklkkynlEELE 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  328 EAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK---LENELANKEA----ILRQMEEKNRQLQERLELAEQKLQQTM 400
Cdd:PRK03918  522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFY 601
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  401 RKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQreKMNEEHNKRLSDTVDRLltesnERL 480
Cdd:PRK03918  602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLEL-----SRE 674
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 333805618  481 QLHLKERMAALEEknvLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:PRK03918  675 LAGLRAELEELEK---RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
265-685 1.96e-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: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEemntKYQrdirEAMAQKEDMEERITTLE 344
Cdd:TIGR02169  160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----RYQ----ALLKEKREYEGYELLKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   345 KRYLSAQREstsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAelaqrIAALTKAE 424
Cdd:TIGR02169  232 KEALERQKE---------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIG 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   425 ERHGNIEErmrhLEGQLEEKNQELQRA-RQREKMNEEHNKrlsdtvdrlltesnerlqlhLKERMAALEEKnvliqeset 503
Cdd:TIGR02169  298 ELEAEIAS----LERSIAEKERELEDAeERLAKLEAEIDK--------------------LLAEIEELERE--------- 344
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   504 frknLEESLHDKERLAEEIEKLRSELDQLKMRTGSLieptiprthldtSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRM 583
Cdd:TIGR02169  345 ----IEEERKRRDKLTEEYAELKEELEDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKREL 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   584 GVRRDEPKVKS--LGDHEwnrtQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAmmLQEQLDAIN 661
Cdd:TIGR02169  409 DRLQEELQRLSeeLADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD--LKEEYDRVE 482
                          410       420
                   ....*....|....*....|....
gi 333805618   662 KEIRLIQEEKESTELRAEEIENRV 685
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERV 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-529 2.40e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  102 EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLF 181
Cdd:PRK03918  315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  182 EHHKAlDEKVRERLRVSLERVSALEEELAAANQEIVALRE---------------------QNVHIQRKMASSEGSTESE 240
Cdd:PRK03918  395 ELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEE 473
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  241 HLEGMEPGQKVHEKRLSNGSIDSTDET--SQIVELQELLEKQNYEMAQMKERLA-ALSSRVGEVEQEAETARKDLIKTEE 317
Cdd:PRK03918  474 KERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEE 553
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  318 MNTKyqrdIREAMAQKEDMEERITTLEKRYLSAQREStsIHDMNDKLE---------NELANKEAILRQMEEKNRQLQER 388
Cdd:PRK03918  554 LKKK----LAELEKKLDELEEELAELLKELEELGFES--VEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEE 627
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  389 LELAEQKLQQTMRKAEtlpeveaELAQRIAALTK--AEERHGNIEERMRHLEGQLEEKNQELqrarqrekmneEHNKRLS 466
Cdd:PRK03918  628 LDKAFEELAETEKRLE-------ELRKELEELEKkySEEEYEELREEYLELSRELAGLRAEL-----------EELEKRR 689
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618  467 DTVDRLLTEsnerlqlhLKERMAALEEKnvlIQESEtfrkNLEESLHDKERLAEEIEKLRSEL 529
Cdd:PRK03918  690 EEIKKTLEK--------LKEELEEREKA---KKELE----KLEKALERVEELREKVKKYKALL 737
PTZ00121 PTZ00121
MAEBL; Provisional
30-541 3.25e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDiESLTGGLAGSKGADP----PEFAA 105
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAakkkAEEAK 1342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEH--LECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEH 183
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  184 HKALDEKVR--ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHE-KRLSNGS 260
Cdd:PTZ00121 1423 AKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEaKKKADEA 1502
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  261 IDSTDETSQIVELQELLEKQNYEMAQMKERlaalsSRVGEVEQEAETARK--DLIKTEEMntKYQRDIREAMAQKEDMEE 338
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEE-----AKKADEAKKAEEKKKadELKKAEEL--KKAEEKKKAEEAKKAEED 1575
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEE---------KNRQLQERLELAEQKLQQTMRKAETLPEV 409
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  410 EAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesnERLQLHLKERMA 489
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-----EELKKAEEENKI 1730
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  490 ALEEknvLIQESETFRKNLEESLHD---KERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:PTZ00121 1731 KAEE---AKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
284-695 5.36e-09

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 60.89  E-value: 5.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   284 MAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEerITTLEKRYLSAQRESTSIHDMNDK 363
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   364 LENELANKEAI-LRQMEEknrqlqerLELAEQKLQQTMRKA-----ETLPEVEAELAQRIAALTKAEERHGNIEERMRHL 437
Cdd:pfam15921  304 IQEQARNQNSMyMRQLSD--------LESTVSQLRSELREAkrmyeDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   438 EGQLEEKNQELQRARQREKMNEEHNKRLSD-------TVDRLLTESNER-----------------LQLHLKERMAALEE 493
Cdd:pfam15921  376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRnmevqrleallkamkseCQGQMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   494 KNVLIQESETFRKNLEESlhdKERLAEEIEKLRSELDQLKmrtgsliepTIPRTHLDTSAELRYSVGSLVDSQSDyrTTK 573
Cdd:pfam15921  456 KNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLE---------SSERTVSDLTASLQEKERAIEATNAE--ITK 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   574 VirrprRGRMGVRRDEPK-VKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIddddRETIFSSMDLLSPSGHSDA--QTLA 650
Cdd:pfam15921  522 L-----RSRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL----RQQIENMTQLVGQHGRTAGamQVEK 592
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 333805618   651 MMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNL 695
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
895-961 5.73e-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: 5.73e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618    895 FAQWDGPTVVAWLELwLGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 961
Cdd:smart00454    1 VSQWSPESVADWLES-IGLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-539 7.79e-09

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 60.12  E-value: 7.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    33 QLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQrQLNSALPQDIESLTGGLAGSKgadppefaaltKELNA 112
Cdd:pfam15921  328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKRE-----------KELSL 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   113 CREQ---LLEKEE----EISELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHK 185
Cdd:pfam15921  396 EKEQnkrLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   186 ALDEKVRERL---RVSLER----VSAL-------EEELAAANQEIVALREQnvhIQRKMASSEG-STESEHLEGMEPGQK 250
Cdd:pfam15921  475 EMLRKVVEELtakKMTLESsertVSDLtaslqekERAIEATNAEITKLRSR---VDLKLQELQHlKNEGDHLRNVQTECE 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   251 VHEKRLSngsidstdETSQIVE-LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREA 329
Cdd:pfam15921  552 ALKLQMA--------EKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   330 MAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPE 408
Cdd:pfam15921  624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMqLKS 703
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEhnkrlsdtvdrLLTESNerlqlhlKERM 488
Cdd:pfam15921  704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE-----------AMTNAN-------KEKH 765
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 333805618   489 AALEEKNVLIQESETFRKnleeslhDKERLAEEIEKLRSELDQLKMRTGSL 539
Cdd:pfam15921  766 FLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANM 809
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
275-556 9.23e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 9.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   275 ELLEKQnyemAQMKERLAALSSRVGEVE-----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLS 349
Cdd:TIGR02168  203 KSLERQ----AEKAERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALtkaeerhgn 429
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--------- 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   430 iEERMRHLEGQLEEKNQELQRARQREKMNEEHnkrlsdtvdrLLTESNERLQLhlkermaaLEEKNVLIQESETFRKNLE 509
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQ----------LETLRSKVAQL--------ELQIASLNNEIERLEARLE 410
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 333805618   510 ESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELR 556
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
291-539 1.12e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  291 LAALSSRVGEVEQ--EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrYLSAQREstsIHDMNDKLENEL 368
Cdd:PRK03918  127 LNAIYIRQGEIDAilESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-FIKRTEN---IEELIKEKEKEL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  369 ANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQ---LEEKN 445
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  446 QELQRARQREKMNEEHNKRLSDTVDRL-----LTESNERLQLHLKERMAALEEKNVLIQESETFRKNLE---ESLHDKER 517
Cdd:PRK03918  283 KELKELKEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHE 362
                         250       260
                  ....*....|....*....|..
gi 333805618  518 LAEEIEKLRSELDQLKMRTGSL 539
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGL 384
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-540 3.33e-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: 3.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHeRSLrmtvvkrqaqspsgvSSEVEVLKALKSLFEhhK 185
Cdd:TIGR04523  171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSL---------------ESQISELKKQNNQLK--D 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   186 ALDEKVRErlrvslerVSALEEELAAANQEIVALREQNVHIQRKMA--SSEGSTESEHLEGMEPGQKVHEKRLSNgsIDS 263
Cdd:TIGR04523  233 NIEKKQQE--------INEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKSEISD--LNN 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREamaqKEDMEERIttl 343
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL--- 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   344 ekrylsaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKA 423
Cdd:TIGR04523  376 -------KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   424 ----EERHGNIEERMRHLEGQ--------------LEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNErlqlhLK 485
Cdd:TIGR04523  449 dsvkELIIKNLDNTRESLETQlkvlsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LK 523
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   486 ERMAALE----EKNVLIQESETFRKNLEESLhDKERLAEEIEKLRSELDQLKMRTGSLI 540
Cdd:TIGR04523  524 EKIEKLEsekkEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLK 581
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
269-472 4.41e-08

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 57.34  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMN-------TKYQRDIREAMAQKEDMEERIT 341
Cdd:COG4372    75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELaaarqnlAKAQQELARLTKQAQDLQTRLK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  342 TL--EKRYLSAQREStsihdmndkLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA 419
Cdd:COG4372   155 TLaeQRRQLEAQAQS---------LQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARRAAA 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 333805618  420 LTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL 472
Cdd:COG4372   226 AQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQL 278
PRK01156 PRK01156
chromosome segregation protein; Provisional
35-481 4.55e-08

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 57.60  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   35 MVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSA-------------LPQDIESLTGGLAGSKGADPP 101
Cdd:PRK01156  244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkYKNDIENKKQILSNIDAEINK 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  102 EFAALTK--ELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHErSLRMtvvKRQAQSPSGVSSEVEVLKALKS 179
Cdd:PRK01156  324 YHAIIKKlsVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-SLKK---KIEEYSKNIERMSAFISEILKI 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  180 LFEHHKALDeKVRERLRVSLERVSAleeELAAANQEIVALREQNVHIQRKMASSEGSTESEhLEGMEPGQKVHEKRLSNG 259
Cdd:PRK01156  400 QEIDPDAIK-KELNEINVKLQDISS---KVSSLNQRIRALRENLDELSRNMEMLNGQSVCP-VCGTTLGEEKSNHIINHY 474
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSrvGEVEQ------EAETARKDL--IKTEEMNTKYQRDIREAMA 331
Cdd:PRK01156  475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKsineynKIESARADLedIKIKINELKDKHDKYEEIK 552
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  332 QK------EDMEERITTLEKryLSAQRESTSIhDMNDKLENELANK----------------------EAILRQMEEKNR 383
Cdd:PRK01156  553 NRykslklEDLDSKRTSWLN--ALAVISLIDI-ETNRSRSNEIKKQlndlesrlqeieigfpddksyiDKSIREIENEAN 629
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  384 QLQERLELAEQK--LQQTMR-KAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEE 460
Cdd:PRK01156  630 NLNNKYNEIQENkiLIEKLRgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
                         490       500
                  ....*....|....*....|.
gi 333805618  461 HNKRLSDTVdrllTESNERLQ 481
Cdd:PRK01156  710 RINELSDRI----NDINETLE 726
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
324-533 7.92e-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: 7.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   324 RDIREAMAQKED----MEERITTLEKRYLSAQRestsIHDMNDKLENelANKEAILRQMEEKNRQLqERLELAEQKLQQT 399
Cdd:TIGR02168  182 ERTRENLDRLEDilneLERQLKSLERQAEKAER----YKELKAELRE--LELALLVLRLEELREEL-EELQEELKEAEEE 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   400 MRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL------ 472
Cdd:TIGR02168  255 LEELTAeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELesklde 334
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618   473 ----LTESNERLQLhLKERMAALEEKnvlIQESETFRKNLEESLHDKErlaEEIEKLRSELDQLK 533
Cdd:TIGR02168  335 laeeLAELEEKLEE-LKEELESLEAE---LEELEAELEELESRLEELE---EQLETLRSKVAQLE 392
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-538 8.20e-08

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 57.03  E-value: 8.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    38 MLDERDRLLDTLRETQESLSLAQQRLQDVIYD-------RDSLQRQLNSALPQ--------------------DIESLTG 90
Cdd:pfam15921  122 MQMERDAMADIRRRESQSQEDLRNQLQNTVHEleaakclKEDMLNDSNTQIEQlrkmmlshegvlqeirsilvDFEEASG 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    91 -----------------GLAGSKgadppEFAALTKELNACREQLLEKEEEISELKAE-RNNTRLLLEH----LECLVSRH 148
Cdd:pfam15921  202 kkiyehdsmstihfrslGSAISK-----ILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEH 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   149 ERSL-----RMTVVKRQAQSpsgVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAA 211
Cdd:pfam15921  277 EVEItglteKASSARSQANS---IQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   212 ANQEIVALReqnvhIQRKMASSEGSTESEHLEGMEPGQKVHEKRLS-----NGSIDSTDETSQIV--ELQELLEKQNYEM 284
Cdd:pfam15921  354 ANSELTEAR-----TERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqNKRLWDRDTGNSITidHLRRELDDRNMEV 428
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   285 AQMKERLAALSSRV-GEVEQEAETARKdliKTEEMNtKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDK 363
Cdd:pfam15921  429 QRLEALLKAMKSECqGQMERQMAAIQG---KNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   364 LEnelaNKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAE-----------------LAQRIAALTKAEER 426
Cdd:pfam15921  505 LQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdkvieiLRQQIENMTQLVGQ 580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   427 HGNIEERMR----HLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAAL----EEKNVLI 498
Cdd:pfam15921  581 HGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE-KVKLVNAGSERLRAVkdikQERDQLL 659
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 333805618   499 QESETFRKNLEESLHDKERLAEEI----EKLRSELDQLKMRTGS 538
Cdd:pfam15921  660 NEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKS 703
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
115-520 8.63e-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: 8.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   115 EQLLEKEEEISELKAERNNTRLL----LEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVE-VLKALKSLFEHHKALDE 189
Cdd:TIGR00606  684 QRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDlKEKEIPELRNKLQKVNR 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   190 KVrERLRVSLERVSAL------EEELAAANQEIVA----LREQNVHIQRKMASSEGSTESEHLEG--MEPGQKVHEKRLS 257
Cdd:TIGR00606  759 DI-QRLKNDIEEQETLlgtimpEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   258 NGSIdstdeTSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:TIGR00606  838 LDTV-----VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   338 ERITTLEKrylSAQRESTSIHDMNDklENELANKEaiLRQMEEKNRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRI 417
Cdd:TIGR00606  913 PLETFLEK---DQQEKEELISSKET--SNKKAQDK--VNDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVN 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   418 AALTKAEERHGNIEERMRHLEGQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDRLLTESNERLQLHLKERMAALEEK 494
Cdd:TIGR00606  984 AQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
                          410       420       430
                   ....*....|....*....|....*....|.
gi 333805618   495 NVLIQESETF-----RKNLEESLHDKERLAE 520
Cdd:TIGR00606 1063 IDLIKRNHVLalgrqKGYEKEIKHFKKELRE 1093
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
36-494 8.95e-08

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 56.65  E-value: 8.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    36 VNMLDERDRLLD-TLRETQESLSLAQQRLQDViydRDSLQRQLNS--ALPQDIESLTGGLAgskgadppefaALTKELNA 112
Cdd:pfam05483  270 ANQLEEKTKLQDeNLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKTIC-----------QLTEEKEA 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   113 CREQLLEKEEE----ISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpsgvsSEVEVLKALKS-----LFEH 183
Cdd:pfam05483  336 QMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEEL 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   184 HKALDEKvrERLRVSLERVSALEEELAAANQEIVAL---REQNVH---IQ------------RKMASSEGSTESEHLEGM 245
Cdd:pfam05483  411 KKILAED--EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQltaiktseehylKEVEDLKTELEKEKLKNI 488
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   246 EPGQKVHEKRLSNGSI--DSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLI---------- 313
Cdd:pfam05483  489 ELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckl 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   314 -KTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMN---------------------DKLENELANK 371
Cdd:pfam05483  569 dKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASA 648
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   372 EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETL--------PEVEAELAQRIAALTKAEERHGN-----IEERMRHLe 438
Cdd:pfam05483  649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIadeavklqKEIDKRCQHKIAEMVALMEKHKHqydkiIEERDSEL- 727
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   439 GQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLT---ESNERLQLHLKERMAALEEK 494
Cdd:pfam05483  728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTAILKDK 786
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
169-533 1.18e-07

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: 56.29  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   169 SEVEVLKALKSLFEHHKALDEKVRERL--RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGME 246
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   247 PGQKV-----HEKRLSNGSIDSTDETSQIVELQELlEKQNYEMAQMKERlaalssrvgeVEQEAETARKDLIKTEEMntk 321
Cdd:pfam17380  346 RERELerirqEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNER----------VRQELEAARKVKILEEER--- 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   322 yQRDIREAMAQKEDMeerittlekrylsaqrestsihdmndKLENELANKEAILRQMEEKNRQLqERLELAEQKLQQTMr 401
Cdd:pfam17380  412 -QRKIQQQKVEMEQI--------------------------RAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV- 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   402 kaETLPEVEAELAQRIAALTKAEERHGNIEERMRH-LEGQLEEKnqelqrarqREKMNEEHNKRlsdtvdrlltesnERL 480
Cdd:pfam17380  463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEER---------KQAMIEEERKR-------------KLL 518
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333805618   481 QLHLKERMAALEEKNVLIQESETFRKNLEesLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLE 569
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1021-1076 1.18e-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: 1.18e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618   1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
193-541 1.57e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.13  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   193 ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMepgQKVHEKRLSNgsidstdetsQIVE 272
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ---LRARIEELRA----------QEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   273 LQELLEKQNYemAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEkrylSAQR 352
Cdd:TIGR00618  279 LEETQERINR--ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ----TLHS 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   353 ESTSIHDMNDKlenELANKEAILRQMEEKN--RQLQERLELAEQKLQQTMRKAETLPE----VEAELAQRIAALTKAEER 426
Cdd:TIGR00618  353 QEIHIRDAHEV---ATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQReqatIDTRTSAFRDLQGQLAHA 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   427 HGNIEERMRHLEGQ----------LEEKNQELQRARQR---EKMNEEHNKRLSDTVDRLLTESNERLQLH------LKER 487
Cdd:TIGR00618  430 KKQQELQQRYAELCaaaitctaqcEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGS 509
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333805618   488 MAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
309-532 1.81e-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: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   309 RKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRY----LSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQ 384
Cdd:TIGR00618  165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   385 LQERLELAEQK------LQQTMRKAETLPEVEAELAQRIAALTKA--EERHGNIEERMRHLEGQLEEKNQELQ-RARQRE 455
Cdd:TIGR00618  245 LTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQsKMRSRA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   456 KMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLH----DKERLAEEIEKLRSELDQ 531
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqQKTTLTQKLQSLCKELDI 404

                   .
gi 333805618   532 L 532
Cdd:TIGR00618  405 L 405
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
220-532 1.89e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 55.55  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   220 REQNVHIQRKMASSEGSTESEHLEGMEPG-QKVH-EKRLSNGSIDSTDETSQIVELQEllEKQNYEMAQMKERLAALSSR 297
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLEEEEAArQKLQlEKVTTEAKIKKMEEDILLLEDQN--NKLQKERKLLEERISEFTSN 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   298 VGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEErittlEKRYLSAqrESTSIHDMNDKLENELANKEAILRQ 377
Cdd:pfam01576  168 LAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEK-----AKRKLEG--ESSDLQEQIAELQAQIAELRAQLAK 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   378 MEEKNRQLQERLE---LAEQKLQQTMRKAET-LPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEK------NQE 447
Cdd:pfam01576  241 KEEELQAALARLEeetAQKNAALKKLRELEAqLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTldttaaQQE 320
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   448 LQRARQRE--------------------KMNEEHNKRLSDTVDRLltESNERLQLHLKERMAALEEKNVLI--------- 498
Cdd:pfam01576  321 LRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQL--EQAKRNKASLEKAKQALESENAELqaelrslqq 398
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 333805618   499 --QESETFRKNLEESLHD-----------KERLAEEIEKLRSELDQL 532
Cdd:pfam01576  399 akQDSEHKRKKLEGQLQElqsrlseserqRAELAEKLSKLQSELESV 445
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
38-422 2.30e-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: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    38 MLDERDRLLDTLRETQESLSLAQQRLQDviydrdsLQRQLnSALPQDIESLTGglagskgadppEFAALTKELNACREQL 117
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSD-------ASRKI-GEIEKEIEQLEQ-----------EEEKLKERLEELEEDL 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   118 LEKEEEISELKAErnntrllLEHLECLVSRHERSLrmtvvkrqaqspSGVSSEVEVLKA--LKSLFEHHKALDEKVRERL 195
Cdd:TIGR02169  747 SSLEQEIENVKSE-------LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEV 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   196 RVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEhlegmepGQKVHEKRLsngsidstdetsQIVELQE 275
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNG------------KKEELEE 868
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   276 LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRD---IREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:TIGR02169  869 ELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKrkrLSELKAKLEALEEELSEIEDPKGEDEE 945
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   353 ESTSIHDMnDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK 422
Cdd:TIGR02169  946 IPEEELSL-EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
114-538 2.30e-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: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   114 REQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRmtvvkRQAQSPSGVSSEVEVLKAL------KSLFEHHK-- 185
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ-----DLTEEKSTLAGEIRDLKDMldvkerKINVLQKKie 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   186 ALDEKVRERLRV---------SLERVSA--------LEEELAAANQEIVALREQNvhiqrkmaSSEGSTESEHLEGMEPG 248
Cdd:pfam10174  405 NLQEQLRDKDKQlaglkervkSLQTDSSntdtalttLEEALSEKERIIERLKEQR--------EREDRERLEELESLKKE 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   249 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQrDIRE 328
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKAH-NAEE 548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   329 AMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME----EKNRQLQERLELAEQKLQQTMRKAE 404
Cdd:pfam10174  549 AVRTNPEINDRIRLLEQEVARYKEESG-------KAQAEVERLLGILREVEneknDKDKKIAELESLTLRQMKEQNKKVA 621
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   405 TLPEVEAELAQRIAALTkaEERHGNIEERMR-HLEGQLEEKNQELQRARQREkmnEEHNKRLSDTV------DRLLTESN 477
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLL--EEARRREDNLADnSQQLQLEELMGALEKTRQEL---DATKARLSSTQqslaekDGHLTNLR 696
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618   478 ERLQLHLKERM--------AALEEKNVLIQEsetfrknLEESLHDKERLAEEIEKLRSELD----QLKMRTGS 538
Cdd:pfam10174  697 AERRKQLEEILemkqeallAAISEKDANIAL-------LELSSSKKKKTQEEVMALKREKDrlvhQLKQQTQN 762
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
30-451 2.38e-07

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 55.49  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    30 HFEQLMVNMLDERDRLLDTLRETQESLSLAQQRlQDVIYDRDS--------LQRQLN---------SALPQDIESLTGG- 91
Cdd:pfam15921  367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTgnsitidhLRRELDdrnmevqrlEALLKAMKSECQGq 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    92 ----LAGSKGADPP--EFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKrQAQSPS 165
Cdd:pfam15921  446 merqMAAIQGKNESleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE-ITKLRS 524
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   166 GVSSEVEVLKALKSLFEHhkaldekvrerLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGM 245
Cdd:pfam15921  525 RVDLKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   246 EPGQKVHEKR--LSNGSIDSTDETSQIVELQELLEKQNYEMAQM----KERLAALSSRVGEVEQ---EAETARKDLIKTE 316
Cdd:pfam15921  594 QLEKEINDRRleLQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQllnEVKTSRNELNSLS 673
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   317 EMNTKYQRDIREamaQKEDMEERITTLEKRYLSAQRE----STSIHDMNDKLENELANKEAILRQMEEKNRQ---LQERL 389
Cdd:pfam15921  674 EDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSEleqtRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKI 750
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618   390 ELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
350-537 3.01e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  350 AQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN 429
Cdd:PRK02224  197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  430 IEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH-------------LKERMAALEE 493
Cdd:PRK02224  277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrDEELRDRLEECrvaaqahneeaesLREDADDLEE 356
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 333805618  494 KNVLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTG 537
Cdd:PRK02224  357 RAEELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
102-533 3.03e-07

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: 55.23  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   102 EFAALTKELNacrEQLLEKEEEISELKAERNNTRLLL--------EHLECLVSRHERSLRMTVVKR---QAQSPSgVSSE 170
Cdd:pfam12128  280 ERQETSAELN---QLLRTLDDQWKEKRDELNGELSAAdaavakdrSELEALEDQHGAFLDADIETAaadQEQLPS-WQSE 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   171 VEVL-KALKSLFEHHKALDEKVrERLRvsLERVSALEEELAAANQEIVALREQnvhIQRKMASSEGsteseHLEGME-PG 248
Cdd:pfam12128  356 LENLeERLKALTGKHQDVTAKY-NRRR--SKIKEQNNRDIAGIKDKLAKIREA---RDRQLAVAED-----DLQALEsEL 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   249 QKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEmAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIRE 328
Cdd:pfam12128  425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEV-------ERLQSELRQ 496
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   329 AMAQKEDMEERITTLEKRYLSAQRESTSIHDMND----KLENELANKEAILRQMEEK--NRQLQERLELAEQKLQQTMRK 402
Cdd:pfam12128  497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLHFLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGG 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   403 AETL-------------------PEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 463
Cdd:pfam12128  577 ELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   464 RLSDTVDRL---LTESNERLQLHLKERMAALE-EKNVLIQESETF-----RKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam12128  657 RLFDEKQSEkdkKNKALAERKDSANERLNSLEaQLKQLDKKHQAWleeqkEQKREARTEKQAYWQVVEGALDAQLALLK 735
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-524 4.03e-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: 54.26  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   106 LTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTvvKRQAQSpsgVSSEVEVLKALKSlfehhK 185
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL--EKQLNQ---LKSEISDLNNQKE-----Q 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   186 ALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIqrkmassegstesehlegmepgqkvhEKRLSNGSIDSTD 265
Cdd:TIGR04523  307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL--------------------------KKELTNSESENSE 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   266 ETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAEtarkdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEK 345
Cdd:TIGR04523  361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   346 RYLSAQREstsIHDmndkLENELANKEAILRQMEEKNRQLQERLEL-------AEQKLQQTMR-------KAETLPEVEA 411
Cdd:TIGR04523  434 TIIKNNSE---IKD----LTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkIKQNLEQKQKelkskekELKKLNEEKK 506
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   412 ELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 490
Cdd:TIGR04523  507 ELEEKVKDLTK---KISSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
                          410       420       430
                   ....*....|....*....|....*....|....
gi 333805618   491 LEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:TIGR04523  584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
1099-1170 7.15e-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: 7.15e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618   1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDEnfdysSLALLLQIPTQNTQARQILEREYNNLLA 1170
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLT-----SEEDLKELGITKLGHRKKILKAIQKLKE 67
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
273-606 7.88e-07

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 53.10  E-value: 7.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDlikteemNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:COG4372    65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETE-------REAARSELQKARQEREAVRQELAAARQNLAKAQQ 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  353 ESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEE 432
Cdd:COG4372   138 ELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  433 RMRHLEGQLEEKNQEL-QRARQREKMNEEHNKRlsdtvdrlltesnerlqlhlKERMAALEEKnvlIQESETFRKNLEES 511
Cdd:COG4372   218 ELARRAAAAQQTAQAIqQRDAQISQKAQQIAAR--------------------AEQIRERERQ---LQRLETAQARLEQE 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  512 LHDKERLAEEIEKLRseLDQLKMRTGSLIEPTIPRThlDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGrmgvRRDEPK 591
Cdd:COG4372   275 VAQLEAYYQAYVRLR--QQAAATQRGQVLAGAAQRV--AQAQAQAQAQAQLLSSANRPAALRLRRSPRRG----RRQRPV 346
                         330
                  ....*....|....*
gi 333805618  592 VKSLGDHEWNRTQQI 606
Cdd:COG4372   347 TRHTTRRRRPATRQS 361
PRK12704 PRK12704
phosphodiesterase; Provisional
367-524 1.32e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  367 ELANKEAIlRQMEEKNRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQ 446
Cdd:PRK12704   34 KEAEEEAK-RILEEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  447 ELQRARQREKMNEEHNKRLSDTVDRLLTESNERLqlhlkERMAAL---EEKNVLIQESEtfrknlEESLHDKERLAEEIE 523
Cdd:PRK12704  111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179

                  .
gi 333805618  524 K 524
Cdd:PRK12704  180 E 180
PTZ00121 PTZ00121
MAEBL; Provisional
240-524 1.75e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  240 EHLEGMEPGQKVHEKRLSNGSIDSTDET-----SQIVELQELL-EKQNYEMAQMKErlaalsSRVGEVEQEAETARKDLI 313
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGkaeakAHVGQDEGLKpSYKDFDFDAKED------NRADEATEEAFGKAEEAK 1104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  314 KTEEMNTKYQRDIREAMAQKEDMeerittlekRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKnRQLQERLELAE 393
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDA---------RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAED 1174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  394 QKLQQTMRKAETLPEVE----AELAQRIAALTKAEERHgNIEERMRHLEgqlEEKNQELQRARQREKMNEEHNKRLSDTV 469
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEEER-KAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618  470 DRLLTESNERLQLHLKERMAAL--EEKnvliQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIkaEEA----RKADELKKAEEKKKADEAKKAEEKKK 1303
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
63-532 1.93e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 52.47  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    63 LQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKgadpPEFAALTKELNACRE---QLLEKEEEISELKAERNNT----R 135
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLE----EETAQKNAALKKLREleaQLSELQEDLESERAARAKAekqrR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   136 LLLEHLECLVSRHERSLRMTVVKRQAQSpsgvSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQE 215
Cdd:pfam01576  296 DLGEELEALKTELEDTLDTTAAQQELRS----KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   216 IV-------ALREQNVHIQRKMAS-SEGSTESEHlegmepGQKVHEKRLSNGSIDSTDETSQIVELQELLEKqnyemaqM 287
Cdd:pfam01576  372 KAslekakqALESENAELQAELRSlQQAKQDSEH------KRKKLEGQLQELQSRLSESERQRAELAEKLSK-------L 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   288 KERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKrylsaqrESTSIHDMndkLENE 367
Cdd:pfam01576  439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSSRLRQLED-------EKNSLQEQ---LEEE 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   368 LANKEAILRQMEEKNRQLQErlelAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERM----RHLEGQLEE 443
Cdd:pfam01576  509 EEAKRNVERQLQTLQAQLSD----LKKKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLektkNRLQQELDD 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   444 KNQELQRARQREKMNEEHNKRLsdtvDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIE 523
Cdd:pfam01576  585 LLVDLDHQRQLVSNLEKKQKKF----DQMLAEEKAISARYAEERDRAEAEAREKETKALSLARALEEALDAKEELERQNK 660

                   ....*....
gi 333805618   524 KLRSELDQL 532
Cdd:pfam01576  661 QLRAEMEDL 669
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-383 2.14e-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: 52.38  E-value: 2.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    41 ERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGG------LAGSKGADPPEFAALTKELNACR 114
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   115 EQLLEKEEEISELKAERNNTRLLLEHLECLVSRhERSLRMTVVKRQAQSpsgVSSEVEVLK-ALKSLFEHHKALDEKVR- 192
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKD-LGEEEQLRVKEKIGE---LEAEIASLErSIAEKERELEDAEERLAk 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   193 --ERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKV--HEKRLSNGSIDSTDETS 268
Cdd:TIGR02169  327 leAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEKLKREINELKR 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYL 348
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 333805618   349 SAQREstsihdmndkleneLANKEAILRQMEEKNR 383
Cdd:TIGR02169  487 KLQRE--------------LAEAEAQARASEERVR 507
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-329 2.32e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.02  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   39 LDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSaLPQDIESLTGGLAgskgadppefaALTKELNACREQLL 118
Cdd:COG1196   736 QSRLEELEEELEELEEELEELQERLEELEEELESLEEALAK-LKEEIEELEEKRQ-----------ALQEELEELEEELE 803
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  119 EKEEEISELKAERNNTRLLLEHLEclVSRHERSLRMTVVKRQAQSPSGVSSEVE-VLKALKSLFEHHKALDEKVRERLRV 197
Cdd:COG1196   804 EAERRLDALERELESLEQRRERLE--QEIEELEEEIEELEEKLDELEEELEELEkELEELKEELEELEAEKEELEDELKE 881
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  198 SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELL 277
Cdd:COG1196   882 LEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEAL 961
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618  278 EKQNY----EMAQMKERLAALSSRVGEVEQEAETARKdliKTEEMNTKYQRDIREA 329
Cdd:COG1196   962 GPVNLraieEYEEVEERYEELKSQREDLEEAKEKLLE---VIEELDKEKRERFKET 1014
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
43-457 3.70e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic 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: 50.84  E-value: 3.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    43 DRLLDTLRETQESLSLAQQRLQDViydRDSLQRQL--NSALPQDIESLTGGLAGSKGadppEFAALTKELNACREQLLEK 120
Cdd:pfam19220   30 SQLIEPIEAILRELPQAKSRLLEL---EALLAQERaaYGKLRRELAGLTRRLSAAEG----ELEELVARLAKLEAALREA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   121 EEEISELKAERNNTRLLLEHLEclvsrherslrmtvvKRQAQspsgvssEVEVLKALKslfEHHKALdekvRERLRVSLE 200
Cdd:pfam19220  103 EAAKEELRIELRDKTAQAEALE---------------RQLAA-------ETEQNRALE---EENKAL----REEAQAAEK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   201 RVSALEEELAAAnQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPgqkvHEKRLSNGSIDSTDETSQIVELQELLEK- 279
Cdd:pfam19220  154 ALQRAEGELATA-RERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERa 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   280 ---QNYEMAQMKERLAALSSRVgeveqEAETARkdLIKTEEMNTkyqrdirEAMAQKEDMEERITTLEKRYLSAQRESTS 356
Cdd:pfam19220  229 eaqLEEAVEAHRAERASLRMKL-----EALTAR--AAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDT 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   357 IHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqqTMRKAetlpeveaeLAQRIAALTKAEERHGNIEERMRH 436
Cdd:pfam19220  295 LERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAE 357
                          410       420
                   ....*....|....*....|....*...
gi 333805618   437 LEGQ-------LEEKNQELQRARQREKM 457
Cdd:pfam19220  358 LTKRfeveraaLEQANRRLKEELQRERA 385
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
260-463 4.36e-06

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 50.49  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEER 339
Cdd:COG4942    30 AFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  340 -------------------------ITTLEKRYLSAQRESTSIHDMN-------DKLENELANKEAILRQMEEKNRQLQE 387
Cdd:COG4942   110 ereqrrrlaeqlaalqrsgrnpppaLLVSPEDAQRSVRLAIYYGALNparaeriDALKATLKQLAAVRAEIAAEQAELTT 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618  388 -RLELAEQKLQQTMRKAETlPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNK 463
Cdd:COG4942   190 lLSEQRAQQAKLAQLLEER-KKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARAR 265
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
264-532 4.63e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 4.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   264 TDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKT-----------EEMNTKYQRDIReamaQ 332
Cdd:TIGR04523   92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFlteikkkekelEKLNNKYNDLKK----Q 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   333 KEDMEERITTLEKrylsaqrESTSIHDMNDKLENELANKE---AILRQMEEKNRQLQ-ERLELAEQKLQQTmrkaETLPE 408
Cdd:TIGR04523  168 KEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLEsQISELKKQNNQLK----DNIEK 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   409 VEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLHLKERM 488
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK 313
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 333805618   489 AALEEKNVLIQESETFRKNLEESLhdkERLAEEIEKLRSELDQL 532
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNS 354
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
265-529 8.46e-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: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   265 DETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVE----QEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERI 340
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   341 TTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAA- 419
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKe 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   420 ----LTKAEERHGNIEERMRHLEGQLEEKN---QELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALE 492
Cdd:pfam02463  319 sekeKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 333805618   493 EKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1021-1072 8.72e-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: 8.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 1072
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
269-541 1.14e-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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQK----------EDMEE 338
Cdd:TIGR04523  132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQ 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAI-------LRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 411
Cdd:TIGR04523  212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   412 ELAQRIAALTKAEERH---------GNIEERMRHLEGQLEEKNQELQRARQ------REKMNEEHNKRlsdTVDRLLTES 476
Cdd:TIGR04523  292 QLKSEISDLNNQKEQDwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENS---EKQRELEEK 368
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   477 NERLQLHLKERMAALEEKNVL----------IQESETFRKNLEESLH----DKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLesqindleskIQNQEKLNQQKDEQIKklqqEKELLEKEIERLKETIIKNNSEIKDLTN 447
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
102-448 1.23e-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: 49.44  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   102 EFAALTKELNACREQLLEKEEEISELKAERNNtrlLLEHLEclvsrhERSLRMTVVKRQAQSPSGVSSEVEVlkALKSLF 181
Cdd:pfam10174  374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIEN---LQEQLR------DKDKQLAGLKERVKSLQTDSSNTDT--ALTTLE 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   182 EhhkALDEKVR--ERLRVSLERVS-ALEEELAAANQEIVALREQNVHIQRKMASSEGSTES--EHLEGMEPGQKVHEKRL 256
Cdd:pfam10174  443 E---ALSEKERiiERLKEQREREDrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDlkEHASSLASSGLKKDSKL 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   257 SNGSIDSTDETSQIVELQELLEK-QNYEMAQMKErlAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKED 335
Cdd:pfam10174  520 KSLEIAVEQKKEECSKLENQLKKaHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   336 MEERITTLEKRYLSaQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQ 415
Cdd:pfam10174  598 KDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKA 676
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 333805618   416 RIAALTKA-EERHGNIE----ERMRHLEGQLEEKNQEL 448
Cdd:pfam10174  677 RLSSTQQSlAEKDGHLTnlraERRKQLEEILEMKQEAL 714
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
184-520 2.52e-05

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 48.53  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  184 HKALDEKVrERLRVSLERVSALEEELaaanqEIVALREQNVHIQRKMASSegsteSEHLEGMEPGQKVHEKRLSNgsids 263
Cdd:COG4477   250 HVNIDSRL-ERLKEQLVENSELLTQL-----ELDEAEEELGLIQEKIESL-----YDLLEREVEAKNVVEENLPI----- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  264 tdetsqiveLQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKdlikteemntkYQRDIREAMAQKEDMEERITTL 343
Cdd:COG4477   314 ---------LPDYLEKAKENNEHLKEEIERVKESYRLAETELGSVRK-----------FEKELKELESVLDEILENIEAQ 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  344 EKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET--LPEVEAELAQRIAalt 421
Cdd:COG4477   374 EVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLERLKSKLHEIKRYMEKsnLPGLPETFLSLFF--- 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  422 kaeerhgNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDtvdrlltESNERLQlhlkerMAALEEKnvLIQES 501
Cdd:COG4477   451 -------TAGHEIQDLMKELSEVPINMEAVSALVDIATEDMNTLED-------ETEEVVE------NAVLAEQ--LIQYG 508
                         330       340
                  ....*....|....*....|..
gi 333805618  502 ETFRK---NLEESLHDKERLAE 520
Cdd:COG4477   509 NRYRSrnaEVAKSLNEAERLFE 530
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
186-529 2.53e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.68  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   186 ALDEKVRERLRV-------SLERVSALEEELAAANqeiVALREQNVHIQRKMASSEGSTES-EHLEGMEPGQKVHEKRLS 257
Cdd:pfam12128  597 ASEEELRERLDKaeealqsAREKQAAAEEQLVQAN---GELEKASREETFARTALKNARLDlRRLFDEKQSEKDKKNKAL 673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   258 NGSIDSTDETSQIVELQE--LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK---DLIKTEEMNTKYQRDiREAMAQ 332
Cdd:pfam12128  674 AERKDSANERLNSLEAQLkqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAK-AELKAL 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   333 KEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQmeekNRQLQERLELAEQKLQQTMRKAET-LPEVEA 411
Cdd:pfam12128  753 ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY----FDWYQETWLQRRPRLATQLSNIERaISELQQ 828
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   412 ELAQRIAaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQR-EKMNEEHnkrlsdtvdrlLTESNERLQLHLKERMAA 490
Cdd:pfam12128  829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEmSKLATLK-----------EDANSEQAQGSIGERLAQ 894
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 333805618   491 LEE-KNVLIQESETFRKNLEE-----SLHDKERLAEEIEKLRSEL 529
Cdd:pfam12128  895 LEDlKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
285-533 2.54e-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: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 48.57  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   285 AQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRylsaqrestsihdmndkl 364
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMELEHKRARIELERKASALARQLERESDRNQELQKRIRLLEKR------------------ 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   365 eneLANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHgnieermrhlEGQLEEK 444
Cdd:pfam05557   64 ---EAEAEEALREQAELNRLKKKNLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRQ----------ELELSST 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   445 NQELQRARQRekmNEEHNKRLSDtvdrlLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAeEIEK 524
Cdd:pfam05557  131 NSELEELQER---LDLQKAKAQE-----AEQLRQNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPE 201

                   ....*....
gi 333805618   525 LRSELDQLK 533
Cdd:pfam05557  202 LERELERLR 210
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
190-533 2.66e-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.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 48.31  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   190 KVRERLRVSLERVSALEEELAAANQEIVALREQNvhiqrkmasSEGSTESEHLEGM--EPGQKVHEKRLSNG-SIDSTDE 266
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESE---------EKNREEVEELKDKyrELRKTLLANRFSYGpAIDELEK 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   267 T-----SQIVELQELLEKQNYEMA-----QMKERLAALSSRVGEVEQEAETARKDLikTEEMNtkyqrDIREAMAQkedM 336
Cdd:pfam06160  154 QlaeieEEFSQFEELTESGDYLEArevleKLEEETDALEELMEDIPPLYEELKTEL--PDQLE-----ELKEGYRE---M 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   337 EERITTLEkrYLSAQRESTSIHDMNDKLENELANKEaiLRQMEEKNRQLQERLElaeqKLQQTMRKaetlpEVEAELaqr 416
Cdd:pfam06160  224 EEEGYALE--HLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERID----QLYDLLEK-----EVDAKK--- 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   417 iaaltKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEH-------NKRLsDTVDRLLTESNERLQLH------ 483
Cdd:pfam06160  288 -----YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENElervrglEKQL-EELEKRYDEIVERLEEKevayse 361
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 333805618   484 LKERMAALEEKNVLIQES-ETFRKNLeESLHDKERLA-EEIEKLRSELDQLK 533
Cdd:pfam06160  362 LQEELEEILEQLEEIEEEqEEFKESL-QSLRKDELEArEKLDEFKLELREIK 412
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
355-465 2.76e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  355 TSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAEL---AQRIA--ALTKAEERHGN 429
Cdd:PRK00409  509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAqqAIKEAKKEADE 588
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 333805618  430 IEERMRHLE--GQLEEKNQELQRARQR-EKMNEEHNKRL 465
Cdd:PRK00409  589 IIKELRQLQkgGYASVKAHELIEARKRlNKANEKKEKKK 627
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
255-494 3.07e-05

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 48.48  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  255 RLSNGSIDSTDETSQIVElqELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrdirEAMAQKE 334
Cdd:COG5281   244 RFASASGESIDKTIKAFS--KLTDDPVNGAKALNRQFHYLTAAQLEQIAALQRAGDTAAAAAAAAEAAA----AMDDRTA 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  335 DMEERITTLEKrylSAQRESTSIHDMNDKLENELANKE--AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLpeveAE 412
Cdd:COG5281   318 RVKENMGTLET---AWDALADAAKKMWDAVLGIGREDKqaALLAAKLAAEKLARVTAQGALNARLKLAQDDLTQ----AE 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  413 LAQRIAALTKAEERHGNieERMRHLEGQLEEKNQELQR------ARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKE 486
Cdd:COG5281   391 LNYAAADQAANQEGALN--AREDEAEVLSTQEERRDILknlladAEKRTARQEELNKALAKAKILQADKAAKAYQEDILQ 468

                  ....*...
gi 333805618  487 RMAALEEK 494
Cdd:COG5281   469 REAQSRGK 476
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
45-538 3.72e-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: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    45 LLDTLRETQES---LSLAQQRLQDVIydrdSLQRQLNSALPQDIESlTGGLAGSKGADPP-----------EFAALTKEL 110
Cdd:pfam10174   58 LKEQYRVTQEEnqhLQLTIQALQDEL----RAQRDLNQLLQQDFTT-SPVDGEDKFSTPElteenfrrlqsEHERQAKEL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   111 NACREQLLEKEEEISE----LKAERNNTRLLLEHLEC-------LVSRHERSLRMTVVKRQAQspsgvssEVEVLKALKS 179
Cdd:pfam10174  133 FLLRKTLEEMELRIETqkqtLGARDESIKKLLEMLQSkglpkksGEEDWERTRRIAEAEMQLG-------HLEVLLDQKE 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   180 LFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVAL----REQNVHIQRKMASSEGSTE--SEHLEGMEPgQKVHE 253
Cdd:pfam10174  206 KENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLerniRDLEDEVQMLKTNGLLHTEdrEEEIKQMEV-YKSHS 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   254 KRLSNgSIDSTDE-----TSQIVELQ---ELLEKQNYEMAQ----MKERLAALSSRVGEVEQEAETARKDLIKTEEMNTK 321
Cdd:pfam10174  285 KFMKN-KIDQLKQelskkESELLALQtklETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNK 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   322 YQ-----------------RDIREAMAQKE------------------DMEERITTLEKRYLSAQRESTSIHDMNDKLEN 366
Cdd:pfam10174  364 KTkqlqdlteekstlageiRDLKDMLDVKErkinvlqkkienlqeqlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   367 ELANKEAIL-RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGN-------IEERMRHLE 438
Cdd:pfam10174  444 ALSEKERIIeRLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlassglkKDSKLKSLE 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   439 GQLEEKNQE-------LQRARQRE---KMNEEHNKRLS---DTVDRLLTESN------ERLQLHLKE----------RMA 489
Cdd:pfam10174  524 IAVEQKKEEcsklenqLKKAHNAEeavRTNPEINDRIRlleQEVARYKEESGkaqaevERLLGILREvenekndkdkKIA 603
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618   490 ALEE-------------KNVLIQESETFRKN---LEESLHDK------------ERLAEEIEKLRSELDQLKMRTGS 538
Cdd:pfam10174  604 ELESltlrqmkeqnkkvANIKHGQQEMKKKGaqlLEEARRREdnladnsqqlqlEELMGALEKTRQELDATKARLSS 680
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
384-541 5.93e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.40  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  384 QLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTK---AEERHGNIEERMRHLEG-----QLEEKNQELQRARQRE 455
Cdd:COG1196   169 KYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERqaeKAERYQELKAELRELELalllaKLKELRKELEELEEEL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  456 KMNEEHNKRLSDTVDRLLTEsNERLQLHLKERMAALEEKNVLIQESETFRKNLEEslhDKERLAEEIEKLRSELDQLKMR 535
Cdd:COG1196   249 SRLEEELEELQEELEEAEKE-IEELKSELEELREELEELQEELLELKEEIEELEG---EISLLRERLEELENELEELEER 324

                  ....*.
gi 333805618  536 TGSLIE 541
Cdd:COG1196   325 LEELKE 330
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
269-419 6.42e-05

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 45.82  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTE----EMNTKYQRDiREAMAQKEDMEE------ 338
Cdd:COG1579    18 EKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLEseiqEIRERIKRA-EEKLSAVKDERElralni 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  339 RITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAET-LPEVEAELAQRI 417
Cdd:COG1579    97 EIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSkREELKEKLDPEL 176

                  ..
gi 333805618  418 AA 419
Cdd:COG1579   177 LS 178
PRK12705 PRK12705
hypothetical protein; Provisional
383-580 7.09e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  383 RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERmrhlegqlEEKNQELQRARQREKMNEEHN 462
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  463 KRLSDTVDRLLTESN----ERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHD--KERLAEEIEKLRSELD-QLKMR 535
Cdd:PRK12705   98 EKLDNLENQLEEREKalsaRELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAelEEEKAQRVKKIEEEADlEAERK 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 333805618  536 TGSLIEPTIPRTHLDTSAELRYSVgslVDSQSDYRTTKVIRRPRR 580
Cdd:PRK12705  178 AQNILAQAMQRIASETASDLSVSV---VPIPSDAMKGRIIGREGR 219
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
196-541 9.24e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 46.80  E-value: 9.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  196 RVSLERVSALEEELAAANQEIVALREQNVHIQRKMA---SSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDEtsQIVE 272
Cdd:COG3096   282 RVHLDQALEFRRELYTSRQQLAAEQYRHVDMSRELAelnGAEGDLEADYQAASDHLNLVQTALRQQEKIERYQA--DLEE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:COG3096   360 LTIRLEEQNEVVEEANERQEENEARAEAAELEVDELKSQL-------ADYQQALDVQQTRAIQYQQAIAALERAKELCHL 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  353 ESTSIHDMNDKLENELANKEAILRQMeeknRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAE-----ERH 427
Cdd:COG3096   433 PDLTADSAEEWLETFQAKEEEATEKL----LSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVAREllregPDQ 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  428 GNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMA-----ALEEKNVLIQEse 502
Cdd:COG3096   509 RHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFCKRQGKNLDAEELEALHQELEALIESLSdsvsnAREQRMALRQE-- 586
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 333805618  503 tfRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIE 541
Cdd:COG3096   587 --QEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFT 623
PRK11281 PRK11281
mechanosensitive channel MscK;
333-532 1.20e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.44  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  333 KEDMEERITTLEKRYLSAQRESTSIHDmndkLENELANKEAILRQmEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA- 411
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQD----LEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  412 ELAQRIAALTkaeerhgnieerMRHLEGQLEEKNQELQRARqrekmneehnKRLSDTVDRLLTESN--ERLQlhlkermA 489
Cdd:PRK11281  113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQ-------A 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 333805618  490 ALEEKNVLIQESETFRKNLEESlhDKERLAEEIEKLRSELDQL 532
Cdd:PRK11281  164 ALYANSQRLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALL 204
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
897-961 1.26e-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 heterooligomerize with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 41.10  E-value: 1.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618   897 QWDGPTVVAWLElWLGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 961
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
188-468 1.40e-04

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 45.87  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  188 DEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGS-TESEHLEGMEPGQKVHEKRLSNGSIDSTDE 266
Cdd:COG4942    47 IAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQiADLNARLNALEVQEREQRRRLAEQLAALQR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  267 TSQIVELQELLekqNYEMAQMKERLAALssrvgevEQEAETARKDLIKTEEMNTKYQRDIREAMAQKedmeerittlekr 346
Cdd:COG4942   127 SGRNPPPALLV---SPEDAQRSVRLAIY-------YGALNPARAERIDALKATLKQLAAVRAEIAAE------------- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  347 ylsaQRESTSihdmndkLENELANKEAILRQMEEKNRQLQERLelaEQKLQQTMRKAETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4942   184 ----QAELTT-------LLSEQRAQQAKLAQLLEERKKTLAQL---NSELSADQKKLEELRANESRLKNEIASAEAAAAK 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 333805618  427 HGNIEERMRHLEgqLEEKNQELQRARQREKMNEEHNKRLSDT 468
Cdd:COG4942   250 AREAAAAAEAAA--ARARAAEAKRTGETYKPTAPEKMLISST 289
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1099-1169 1.48e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618  1099 VLVWSNDRVIRWIQAIGLREYANNILESGVHG--SLIALDENFdysslalLLQIPTQNTQARQILEREYNNLL 1169
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGaeLLLRLTLED-------LKRLGITSVGHRRKILKKIQELK 66
mukB PRK04863
chromosome partition protein MukB;
179-465 1.63e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  179 SLFEHHKALDEKVR--ERLRVSLERVSALEEELAAA---NQEIVALREQNVHIQRKMASSEGSTE--SEHLEGMEPGQKV 251
Cdd:PRK04863  797 ELAERYATLSFDVQklQRLHQAFSRFIGSHLAVAFEadpEAELRQLNRRRVELERALADHESQEQqqRSQLEQAKEGLSA 876
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  252 HEKRLsnGSIDSTDETSQIVELQELLEkQNYEMAQMKERLAALSSRVGEVEQEAETARKDliktEEMNTKYQRDIREAMA 331
Cdd:PRK04863  877 LNRLL--PRLNLLADETLADRVEEIRE-QLDEAEEAKRFVQQHGNALAQLEPIVSVLQSD----PEQFEQLKQDYQQAQQ 949
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  332 QKEDMEERITTL----EKR----YLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKA 403
Cdd:PRK04863  950 TQRDAKQQAFALtevvQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618  404 ETLPEVEAELAQRIAALT---------KAEERHGNIEERMRHLEGQleeKNQ-ELQRARQREKMNEEhNKRL 465
Cdd:PRK04863 1030 DAKRQMLQELKQELQDLGvpadsgaeeRARARRDELHARLSANRSR---RNQlEKQLTFCEAEMDNL-TKKL 1097
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
290-549 1.65e-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.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 45.62  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   290 RLAALSSRVGEVEQEAET-----ARKDLIKTEEMNTKYQRDIR-------EAMAQKEDMEERITTLEKRY------LSAQ 351
Cdd:pfam06160   61 SLPDIEELLFEAEELNDKyrfkkAKKALDEIEELLDDIEEDIKqileeldELLESEEKNREEVEELKDKYrelrktLLAN 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   352 RES--TSIhdmnDKLENELANKEAILRQMEEKN--------RQLQERLELAEQKLQQTMRK--------AETLPEVEAEL 413
Cdd:pfam06160  141 RFSygPAI----DELEKQLAEIEEEFSQFEELTesgdyleaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEEL 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   414 AQRIAALTKAEER--HGNIEERMRHLEGQLEE-----KNQELQRArqrEKMNEEHNKRLSDTVDRLLTESNERLQLH--- 483
Cdd:pfam06160  217 KEGYREMEEEGYAleHLNVDKEIQQLEEQLEEnlallENLELDEA---EEALEEIEERIDQLYDLLEKEVDAKKYVEknl 293
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618   484 --LKERMAALEEKNVLIQE-----SETFRKNlEESLHDKERLAEEIEKLRSELDQLKMRtgsLIEPTIPRTHL 549
Cdd:pfam06160  294 peIEDYLEHAEEQNKELKEelervQQSYTLN-ENELERVRGLEKQLEELEKRYDEIVER---LEEKEVAYSEL 362
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
273-535 1.66e-04

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


Pssm-ID: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 45.65  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   273 LQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLiktEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQR 352
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKVEELEEKYKELSR 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   353 ESTSIHdmndklenelANKEAILRQMEEKNRQLQErLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEE-RHGNIE 431
Cdd:pfam07888  109 SGEELA----------EEKDALLAQRAESEARIRE-LEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEaERKQLQ 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   432 ERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRL---LTESNERLQLH--LKERMAALEEK-NVLIQESETFR 505
Cdd:pfam07888  178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqkLTTAHRKEAENeaLLEELRSLQERlNASERKVEGLG 257
                          250       260       270
                   ....*....|....*....|....*....|
gi 333805618   506 KNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:pfam07888  258 EELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
278-491 1.75e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 225177 [Multi-domain]  Cd Length: 548  Bit Score: 45.59  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  278 EKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQ-RDIREAMAQKEDMEERITTLEKRYLSAqrESTS 356
Cdd:COG2268   246 KLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETRREAEQaEILAEQAIQEEKAQAEQEVQHAKALEA--REMR 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  357 IHDMNDKLENELANKE---AILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV-EAELAQRIAALTKAE-------- 424
Cdd:COG2268   324 VGLIERQKETELEPQErsyFINAAQRQAQEEAKAAANIAEAIGAQAEAAVETARETeEAERAEQAALVAAAEaaeqeqve 403
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618  425 --ERHGNIEERMRH------LEGQLEEKNQELQRARQReKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAAL 491
Cdd:COG2268   404 iaVRAEAAKAEAEAqaaeikAEAEAIREKGKAEAEAKR-ALAEAIQVLGDAAAAELFKALVQALPEVAEEAAQPM 477
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
189-453 2.07e-04

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 45.13  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  189 EKVRERLRVSLERVSALEEE---------LAAANQEIVALREQNvHIQRKMASSEGSTESehLEGMEPgQKVHEKRLSNG 259
Cdd:COG3206   141 DDLLESLKVLRAGRSRVIELsytsndpklAAKLANALAQAYLAD-QLEAQLEAFRRASDS--LDERLE-ELRARLQEAEA 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  260 SIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTeemntkyqrdiREAMAQKEDMEER 339
Cdd:COG3206   217 QVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLLPLG-----------REAAALREVLESP 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  340 -ITTLEKRYLSAQREstsIHDMNDKLENELANKEAILRQMEEKNRQLQERLelaeQKLQQTMRKAETLPEV-EAELAQRI 417
Cdd:COG3206   286 tIQDLRQQYAQVRQQ---IADLSTELGAKHPQLVALEAQLAELRQQIAAEL----RQILASLPNELALLEQqEAALEKEL 358
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 333805618  418 AALTKAEERHGNIEERMRHLEGQLEEK----NQELQRARQ 453
Cdd:COG3206   359 AQLKGRLSKLPKLQVQLRELEREAEAArslyETLLQRYQE 398
pepcterm_ChnLen TIGR03007
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ...
200-415 2.36e-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: 45.04  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   200 ERVSALEEELAAANQEIVALREQNVhiqrkmassegstesehleGMEPGQkvhekrlsngsidSTDETSQIVELQELLEK 279
Cdd:TIGR03007  168 EQIKTYEKKLEAAENRLKAFKQENG-------------------GILPDQ-------------EGDYYSEISEAQEELEA 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   280 QNYEMAQMKERLAALSSRVGEVEQEAETARKDL-----IKTEEMNTKYQR----------DIREAMAQKEDMEERITTLE 344
Cdd:TIGR03007  216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnseldGRIEALEKQLDAlrlrytdkhpDVIATKREIAQLEEQKEEEG 295
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333805618   345 KRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLElaeqklqQTMRKAETLPEVEAELAQ 415
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 ...
272-503 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   272 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKryLSAQ 351
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKE--INEK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   352 RESTSIHDM---NDKLENELANKEAILRQMeeKNRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRIAALTKAeerhg 428
Cdd:pfam06008  105 VATLGENDFalpSSDLSRMLAEAQRMLGEI--RSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKA----- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   429 nIEERMRHLEGQLEEKNQELQ--------RARQREKMNEEHNKRLSDTVDRLLT--ESNERLQLHLKERMAALEEKNVLI 498
Cdd:pfam06008  174 -LANALRDSLAEYEAKLSDLRellreaaaKTRDANRLNLANQANLREFQRKKEEvsEQKNQLEETLKTARDSLDAANLLL 252

                   ....*
gi 333805618   499 QESET 503
Cdd:pfam06008  253 QEIDD 257
RmuC COG1322
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ...
372-533 3.19e-04

DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 44.69  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  372 EAILRQMEEKNRQLQERLELAEqKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE-------EK 444
Cdd:COG1322    14 LVNLAFIRQLLLRLGRLEQMLG-ELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELKARLQqqllqsrEQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  445 NQELQRARQR---------EKMNEEHNKRLSDTVDrlltESNERLQLHLKERMAALEEKnVLIQESETFRKNLEEsLHDK 515
Cdd:COG1322    93 LQLLIESLAQlssefqelaNEIFEELNRRLAELNQ----QNLKQLLKPLREVLEKFREQ-LEQRIHESAEERSTL-LEEI 166
                         170
                  ....*....|....*...
gi 333805618  516 ERLAEEIEKLRSELDQLK 533
Cdd:COG1322   167 DRLLGEIQQLAQEAGNLT 184
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
364-535 4.35e-04

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 44.42  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  364 LENELANKEAILRQMEEKNRQLQERlELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEE 443
Cdd:COG4487    47 FEKEANEKRAQYRSAKKKELSQLEE-QLINQKKEQKNLFNEQIKQFELALQDEIAKLEALELLNLEKDKELELLEKELDE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  444 KNQELQRARQReKMNEEHNKRLSDTVDRLLTESNERlqlhlkermaalEEKNVLIQESETFRKNLEESLHDKE--RLAEE 521
Cdd:COG4487   126 LSKELQKQLQN-TAEIIEKKRENNKNEERLKFENEK------------KLEESLELEREKFEEQLHEANLDLEfkENEEQ 192
                         170
                  ....*....|....
gi 333805618  522 IEKLRSELDQLKMR 535
Cdd:COG4487   193 RESKWAILKKLKRR 206
PRK01156 PRK01156
chromosome segregation protein; Provisional
41-568 4.53e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.51  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   41 ERDRLLDTLRETqESLSLAQQRLQDVI-----------YDRDSLQRQLNsalpqDIESLTGGLAgskgADPPEFAALTKE 109
Cdd:PRK01156  150 QRKKILDEILEI-NSLERNYDKLKDVIdmlraeisnidYLEEKLKSSNL-----ELENIKKQIA----DDEKSHSITLKE 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  110 LNACREQLLEKEEEISELKAERNNtrllLEHLECLVSRHERSLRmtvvkrqaQSPSGVSSEVEVLKALKSLFEHHKALDE 189
Cdd:PRK01156  220 IERLSIEYNNAMDDYNNLKSALNE----LSSLEDMKNRYESEIK--------TAESDLSMELEKNNYYKELEERHMKIIN 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  190 ----KVRERLRVSLERVSALE---EELAAANQEIvalreQNVHIQRKMASSEGSTESEHLEgMEPGQKVHEKRLSNGSID 262
Cdd:PRK01156  288 dpvyKNRNYINDYFKYKNDIEnkkQILSNIDAEI-----NKYHAIIKKLSVLQKDYNDYIK-KKSRYDDLNNQILELEGY 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  263 STDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDL----IKTEEMNTK---YQRDIREAMAQKED 335
Cdd:PRK01156  362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELneinVKLQDISSKvssLNQRIRALRENLDE 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  336 MEERITTLEKR--------YLSAQRESTSIHDMNDK---LENELANKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKA 403
Cdd:PRK01156  442 LSRNMEMLNGQsvcpvcgtTLGEEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEY 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  404 ETLPEVEAELAQ---RIAALTKAEERHGNIEERMRHLE-GQLEEKNQELQRA-RQREKMNEEHNKRLSDTVDRLLTESNE 478
Cdd:PRK01156  522 NKIESARADLEDikiKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLES 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  479 RLQlhlkERMAALEEKNVLIQESETFRKNLEESLHDKERLAEE----IEKLRSELDQLKMRTGSL--IEP---TIPRTHL 549
Cdd:PRK01156  602 RLQ----EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEnkilIEKLRGKIDNYKKQIAEIdsIIPdlkEITSRIN 677
                         570
                  ....*....|....*....
gi 333805618  550 DTSAELRYSVGSLVDSQSD 568
Cdd:PRK01156  678 DIEDNLKKSRKALDDAKAN 696
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
150-453 4.73e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 44.25  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  150 RSLRMTVVK--------RQAQSPSGVSSEVevLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE 221
Cdd:COG4372    67 RNLRSGVFQlddirpqlRALRTELGTAQGE--KRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTK 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  222 QNVHIQRKMassegstesehlegmepGQKVHEKRLSNGSIDSTDETSQivELQELLEkqnyemaQMKERLAALSSRVGEV 301
Cdd:COG4372   145 QAQDLQTRL-----------------KTLAEQRRQLEAQAQSLQASQK--QLQASAT-------QLKSQVLDLKLRSAQI 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  302 EQEAetarkdlikteemntkyqrdiREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK 381
Cdd:COG4372   199 EQEA---------------------QNLATRANAAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRER 257
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618  382 NRQLQeRLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIeERMRHLEGQLEEKNQELQRARQ 453
Cdd:COG4372   258 ERQLQ-RLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAA-QRVAQAQAQAQAQAQLLSSANR 327
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
300-526 4.80e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  300 EVEQEAET-----ARKDLIKTEEMNTKYQRD---IREAMA----QKEDMEERITTLEKRYLSAQRE----STSIHDMNDK 363
Cdd:PRK04778   90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQelleSEEKNREEVEQLKDLYRELRKSllanRFSFGPALDE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  364 LENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRI-AALTKAEE------------ 425
Cdd:PRK04778  170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKAgyrelveegyhl 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  426 RHGNIEERMRHLEGQLEEKNQELQR---ARQREKmNEEHNKRLSDTVDRLLTEsnerlqlhlkerMAAleeKNVLIQESE 502
Cdd:PRK04778  250 DHLDIEKEIQDLKEQIDENLALLEEldlDEAEEK-NEEIQERIDQLYDILERE------------VKA---RKYVEKNSD 313
                         250       260
                  ....*....|....*....|....
gi 333805618  503 TFRKNLEESLHDKERLAEEIEKLR 526
Cdd:PRK04778  314 TLPDFLEHAKEQNKELKEEIDRVK 337
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
193-620 4.90e-04

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


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 44.35  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  193 ERLRVSLERVsalEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEK--RLSNGSID----STDE 266
Cdd:COG5192   363 EKMKMQLQEI---EQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEEtsREDELSFDdsdvSTSD 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEvEQEAETARKDLIKTEEMNTkyQRDIREAMAQKEDMEERITTlEKR 346
Cdd:COG5192   440 ENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFD-ESEGNLRWKEGLASKLAYS--QSGKRGRNIQKIFYDESLSP-EEC 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  347 YLSAQRESTSIHDMNDKLENElanKEAILRQMEEKNRQLQERLE-LAEQKLQQTMRKAETLPEVEAELAQriAALTKAEE 425
Cdd:COG5192   516 IEEYKGESAKSSESDLVVQDE---PEDFFDVSKVANESISSNHEkLMESEFEELKKKWSSLAQLKSRFQK--DATLDSIE 590
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  426 RHgniEErmrhLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEK---NVLIQESE 502
Cdd:COG5192   591 GE---EE----LIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEElrgNFELEERG 663
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  503 TFRKN-LEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPT------------IPRTHLDTSaELRYSV--GSLVDSQS 567
Cdd:COG5192   664 DPEKKdVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYragryvrivlshVPLEFVDEF-NSRYPIvlGGLLPAEK 742
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 333805618  568 DYRTTKV-IRRPRRGRMGVRRDEPKVKSLGdheWNRTQQIGVLSSHPFESDTEM 620
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 ...
898-956 5.02e-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: 5.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618  898 WDGPTVVAWLELWLGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 956
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
272-535 5.78e-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: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   272 ELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIRE--AMAQKEDMEERITTLE--KRY 347
Cdd:pfam13868   56 ALEEEEEKEEERKEERKQYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREeiDEF 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   348 LSAQRESTSIHDMNDKLENElANKEAILRQMEEKNRQLQERLELAEQK----------LQQTMRKAETLPEVEAELAQ-- 415
Cdd:pfam13868  136 NEEQAKWKELEKEEEKEEDL-RILEYLKEKAEREEEREAERREIKEEKereiarlraqQEKAQDEKAERDELRAKLYQee 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   416 -----RIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAA 490
Cdd:pfam13868  215 qerkwRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRREKRLEHRRE 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 333805618   491 LEEknvLIQE-SETFRKNLEESLHDKERLAEEIEKLRSELDQLKMR 535
Cdd:pfam13868  295 LEK---QIEErERQRAAEREEELEEGERLREEEAERRERIEEERQK 337
PTZ00121 PTZ00121
MAEBL; Provisional
182-529 5.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  182 EHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALRE-QNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGS 260
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE 1247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  261 IDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARK--DLIKTEEMNTKYQ--RDIREAMAQKEDM 336
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAEeaKKADEAKKKAEEA 1327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  337 EERITTLEKRYLSAQREStsihdmndklenELANKEAilRQMEEKNRQLQERLELAEQKLQQTMRKAEtlpeveaELAQR 416
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAA------------EAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKAD-------AAKKK 1386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  417 IAALTKAEERHGNIEERMRHLEgQLEEKNQELQRARQREKMNEEhnKRLSDTVDRLLTESN--ERLQLHLKERMAA--LE 492
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKkaDEAKKKAEEAKKAeeAK 1463
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 333805618  493 EKNVLIQESETFRKNLEESLHDKE--RLAEEIEKLRSEL 529
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEA 1502
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
267-532 6.31e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  267 TSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLE-- 344
Cdd:PRK04778  111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTes 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  345 ------KRYLSAQRESTS------------IHDMNDKLENELANKEAILRQMEEKN-----RQLQERLELAEQKLQQTMR 401
Cdd:PRK04778  191 gdyveaREILDQLEEELAaleqimeeipelLKELQTELPDQLQELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLA 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  402 KAETLpeveaelaqriaALTKAEERHGNIEERMRHLEGQLE---------EKNQElqRARQREKMNEEHNKRLSDTVDRL 472
Cdd:PRK04778  271 LLEEL------------DLDEAEEKNEEIQERIDQLYDILErevkarkyvEKNSD--TLPDFLEHAKEQNKELKEEIDRV 336
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618  473 -----LTESNERLQLHLKERMAALEEKNVLIQE---------SETfRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:PRK04778  337 kqsytLNESELESVRQLEKQLESLEKQYDEITEriaeqeiaySEL-QEELEEILKQLEEIEKEQEKLSEMLQGL 409
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
362-536 6.73e-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: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  362 DKLENELANKEAILRQME------------EKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIaaltkaEERHGN 429
Cdd:cd00176    10 DELEAWLSEKEELLSSTDygddlesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI------QERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  430 IEERMRHLEGQLEEKNQELQRARQREKMNEEH---NKRLSDTVDRLLTESN-------ERLQLHLKERMAALEEKNVLIQ 499
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQFFRDAddlEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 333805618  500 ESETFRKNLEESLH--DKERLAEEIEKLRSELDQLKMRT 536
Cdd:cd00176   164 SLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELA 202
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
177-448 7.52e-04

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: 44.06  E-value: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   177 LKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQnVHIQRKMASSEGSTESEHLEGMEPGQKVHEKrl 256
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-- 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   257 sngsidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETaRKDLIKtEEMNTKYQRDIREAMAQKEDM 336
Cdd:pfam12128  337 --------ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIK-EQNNRDIAGIKDKLAKIREAR 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   337 EERITTLEKRYlsAQRESTSIHDMN-DKLENELANKEAILRQMEEKNR---------------QLQERLELAEQKLQQTM 400
Cdd:pfam12128  407 DRQLAVAEDDL--QALESELREQLEaGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqleNFDERIERAREEQEAAN 484
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 333805618   401 RKAETLpevEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 448
Cdd:pfam12128  485 AEVERL---QSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
300-533 8.89e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   300 EVEQEAETARKdlikteEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTsihdmndKLENELANKEAILRQME 379
Cdd:pfam05483  201 ELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESR 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   380 EKNRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   456 KMNEEHNKRLSDTVDRLLTESNERLQLH---LKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:pfam05483  348 SFVVTEFEATTCSLEELLRTEQQRLEKNedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427

                   .
gi 333805618   533 K 533
Cdd:pfam05483  428 E 428
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
386-524 9.77e-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: 9.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   386 QERLELAEQKLQQtmrkaetLPEVEAELAQRIAALTKaeeRHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 465
Cdd:pfam12718   13 QERAEELEEKVKE-------LEQENLEKEQEIKSLTH---KNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKI 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   466 sdtvdRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEK 524
Cdd:pfam12718   83 -----QLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEE 136
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
486-544 1.14e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  486 ERMAALEEKNV-LIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKmrTGSLIEPTI 544
Cdd:PRK03992    1 ERLEALEERNSeLEEQIRQLELKLRDLEAENEKLERELERLKSELEKLK--SPPLIVATV 58
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
320-533 1.19e-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: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   320 TKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIhDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQK---- 395
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllq 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   396 -----LQQTMRKAETLPEVEAELAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRlsdtVD 470
Cdd:pfam02463  244 ellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEK---EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KL 316
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333805618   471 RLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
122-455 1.21e-03

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


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 43.29  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  122 EEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSG----VSSEVEVLKALKSLFEHHKALDEKVRERL-- 195
Cdd:COG4717   134 QEIHELNSKGILGYLLFSGTSGSPASTKLLEVLNKEADSLYKPSGrnpqINQLLEKLKQERNEIDEAEKEYATYHKLLes 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  196 -RVSLERVSALEEELAAANQEIVALR---EQNVHIQRKMASSEGSTESEHLEGMEPGQKVH--EKRLSNGSIDSTDETSQ 269
Cdd:COG4717   214 rRAEHARLAELRSELRADRDHIRALRdavELWPRLQEWKQLEQELTRRREELATFPRDGVLrlEKREAHLQKTEAEIDAL 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  270 IVELQELLEKQNyEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNtkyQRDIREAMAQKEDMEERITTLEKRYLS 349
Cdd:COG4717   294 LVRLAELKDLAS-QLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGI---EADLRDKEEAAGNGFEAERVHDLRSLE 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  350 AQRESTSIHDMNDKLENELANK--EAILRQME-EKNRQLQERLELAEQKLQQtmrkaETLPEVEAELAQRIAALTKAEER 426
Cdd:COG4717   370 CMLRYQSSQRELKQTEAAYCKRldEKRLFEDEaEEEARQRLADDEEEVRAGD-----EAREEKIAANSQVIDKEEVCNLY 444
                         330       340
                  ....*....|....*....|....*....
gi 333805618  427 HGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:COG4717   445 DRRDTAWQKQRFLREKQTAFERQKTEHTK 473
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
268-420 1.28e-03

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


Pssm-ID: 433526 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   268 SQIVELQELLEKQNYEMA-------QMKERLAALSSRVGEVEQEAETARKD---LIKTEEMNTKYQRDIREAMAQKEDME 337
Cdd:pfam13851   33 EEIAEMKKKEERNEKLMSeiqqenkRLTEPLQKAQEEVEELRKQLENYEKDkqsLKNLKARLKVLEKELKDLKWEHEVLE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   338 ERITTLEKRY--LSAQREStSIHDMNDKLENE---LANK-EAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEA 411
Cdd:pfam13851  113 QRFEKVERERdeLYDKFEA-AIQDVQQKTGLKnllLEKKlQALGETLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLE 191

                   ....*....
gi 333805618   412 ELAQRIAAL 420
Cdd:pfam13851  192 SKNQLIKDL 200
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
333-536 1.38e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 41.85  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   333 KEDMEERITTLEKRYLSAQrestsihDMNDKLENELANKEAILRQMEEKNRQLQE---RLELAEQKLQQTMRKAETLPEV 409
Cdd:pfam00769    1 REEAEREKQELEERLKQYE-------EETRKAQEELEESEETAELLEEKLRVAEEeaeLLEQKAQEAEEEKERLEESAEM 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   410 EAE----LAQRIAALTKAEERhgnIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLK 485
Cdd:pfam00769   74 EAEekeqLERELREAQEEVAR---LEEESERKEEEAERLQEELEEAREEEEEAKEKLLAASTSPSHHHSEESENEDDEEE 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618   486 ERM-----AALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRT 536
Cdd:pfam00769  151 EESyeggsAELSNDGDMDQLSDRIEEERVTEAEKNERLQKQLKALKSELAQARDET 206
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
152-691 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   152 LRMTVVKRQAQspsgVSSEVEVLKALKSLFEHHKALDEKVRErlrvSLERVSALEEELAAANQEIVALREQNVHIQRKMA 231
Cdd:TIGR00606  222 IRDQITSKEAQ----LESSREIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKME 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   232 SSEGSTESEHLEgmepgqkVHEKRLSNGSidstDETSQIVELQELLEKQNYEMAQMKERLAALSSRVG------EVEQEA 305
Cdd:TIGR00606  294 KVFQGTDEQLND-------LYHNHQRTVR----EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrlqlqaDRHQEH 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   306 ETARKDLIKTEEMNTKY---------QRDIREAMA-QKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAIL 375
Cdd:TIGR00606  363 IRARDSLIQSLATRLELdgfergpfsERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   376 RQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEErHGNIEERMRHLEGQLEEKNQELQRARQRE 455
Cdd:TIGR00606  443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-NSLTETLKKEVKSLQNEKADLDRKLRKLD 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   456 KMNEEHNkRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETF--RKNLEESLH----DKERLAEEIEKLRSEL 529
Cdd:TIGR00606  522 QEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnKKQLEDWLHskskEINQTRDRLAKLNKEL 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   530 DQLKMRTGSLIEPTIPRTHLDTSAELR-YSVGSLVDSQSDY-RTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIG 607
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSSYEDKlFDVCGSQDEESDLeRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   608 VLSSHPFESDTEMSDIDDDdretiFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVAS 687
Cdd:TIGR00606  681 PVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755

                   ....
gi 333805618   688 VSLE 691
Cdd:TIGR00606  756 VNRD 759
HOOK pfam05622
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ...
169-290 1.61e-03

HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.


Pssm-ID: 428548 [Multi-domain]  Cd Length: 526  Bit Score: 42.35  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   169 SEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALE---EELAAANQEIVALREQNVHIQRKM---------ASSEGS 236
Cdd:pfam05622  300 SEREKLTELQALLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLeehleklheAQEELQ 379
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333805618   237 TESEHLEGMEPGQkvhekrlsngsidsTDETSQIVELQELLEKQNYEMAQMKER 290
Cdd:pfam05622  380 KKKEQLEELEPKV--------------DSNLQKIDELQEALRKKDEDMKAMEER 419
COG5022 COG5022
Myosin heavy chain [General function prediction only];
309-532 1.74e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  309 RKDLIKTEEMNTKYQRDIREAMAQKEdMEERITTLEkrylsaqreSTSIHdmNDKLENELANKEAILRQMEEKNRQLQER 388
Cdd:COG5022   809 RKEYRSYLACIIKLQKTIKREKKLRE-TEEVEFSLK---------AEVLI--QKFGRSLKAKKRFSLLKKETIYLQSAQR 876
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  389 LELAEQK---LQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIE-----ERMRHLEGQLEEKNQELQRARQREKmNEE 460
Cdd:COG5022   877 VELAERQlqeLKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGPSIEYVK-LPE 955
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333805618  461 HNKRLsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQL 532
Cdd:COG5022   956 LNKLH--EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEV 1025
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
299-514 2.26e-03

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 41.86  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  299 GEVEQEAETARKdliKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQREStsihdmndklenELANKEAILRQM 378
Cdd:COG3064    65 GRIQSQQSSAKK---GEQQRKKKEEQVAEELKPKQAAEQERLKQLEKERLKAQEQQ------------KQAEEAEKQAQL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  379 EEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMN 458
Cdd:COG3064   130 EQKQQEEQARKAAAEQKKKAEAAKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKA 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618  459 EEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEtfRKNLEESLHD 514
Cdd:COG3064   210 EAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAE--RKAAAAALDD 263
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
259-442 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  259 GSIDSTDETSQIVELQELLEKQNYEMAQM---------KERLAALSSRVGEVEQEAETARKDLikteemnTKYQRDIrea 329
Cdd:cd22656    82 AQNAGGTIDSYYAEILELIDDLADATDDEeleeakktiKALLDDLLKEAKKYQDKAAKVVDKL-------TDFENQT--- 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  330 MAQKEDMEERITTLEKRYlsaQRESTSIHDMN-DKLENELAN-KEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLP 407
Cdd:cd22656   152 EKDQTALETLEKALKDLL---TDEGGAIARKEiKDLQKELEKlNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 333805618  408 EVEAELAQRIAALTKAEERHGNIEERMRHLEGQLE 442
Cdd:cd22656   229 AADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
278-486 2.59e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 41.08  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   278 EKQNYEMAQmkerlaalssRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSI 357
Cdd:pfam00769    5 EREKQELEE----------RLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEME 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   358 HDMNDKLENELANKEA-ILRQMEEKNR------QLQERLELAEQKLQQTMRKAETLPEVEaelaqriaaltkaeerHGNI 430
Cdd:pfam00769   75 AEEKEQLERELREAQEeVARLEEESERkeeeaeRLQEELEEAREEEEEAKEKLLAASTSP----------------SHHH 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618   431 EErmrHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT--VDRL-LTESNERLQLHLKE 486
Cdd:pfam00769  139 SE---ESENEDDEEEEESYEGGSAELSNDGDMDQLSDRieEERVtEAEKNERLQKQLKA 194
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1021-1076 2.69e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 37.63  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 333805618  1021 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 1076
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
PRK12704 PRK12704
phosphodiesterase; Provisional
383-531 2.75e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  383 RQLQERLELAEQKLQQTMRKAETlpevEAELAQRIAALTKAEERHgnieERMRHLEGQLEEKNQELQRARQREKMNEEHn 462
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEEN- 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333805618  463 krlsdtvdrlltesnerlqlhLKERMAALEEKNvliQESETFRKNLEESLHDKERLAEEIEKLRSELDQ 531
Cdd:PRK12704   98 ---------------------LDRKLELLEKRE---EELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
253-434 3.42e-03

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 40.86  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  253 EKRLSNGSIDSTDetSQIVELQEllEKQNYEmaqmkERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAmaq 332
Cdd:COG3883    25 FAALLSDKIQNQD--SKLSELQK--EKKNIQ-----NEIESLDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAEL--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  333 KEDMEERITTLEKR------------YLSAQRESTSIHDMNDKL--------------------ENELANKEAILrqmEE 380
Cdd:COG3883    93 KENIVERQELLKKRaramqvngtatsYIDVILNSKSFSDLISRVtaisvivdadkkileqqkedKKSLEEKQAAL---ED 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333805618  381 KNRQLQERLELAEQKLQQ---------------TMRKAETLPEVEAELAQR-----IAALTKAEERHGNIEERM 434
Cdd:COG3883   170 KLETLVALQNELETQLNSlnsqkaeknaliaalAAKEASALGEKAALEEQKalaeaAAAEAAKQEAAAKAAAQE 243
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
171-534 3.68e-03

Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 41.51  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  171 VEVLKALKSLFEHHKALDEKVRERLRV----------SLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESE 240
Cdd:COG5185   203 VRLIIKLDMCLQPLKTLDQQDRYELMVekllfdyfteSYKSFLKLEDNYEPSEQELKLGFEKFVHIINTDIANLKTQNDN 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  241 HLEGMEPGQKVHEKrlsngsIDSTDETSQivELQELLEKQNYEMAQMKERLaalSSRVGEVEQEAEtarkDLIKTEEMNT 320
Cdd:COG5185   283 LYEKIQEAMKISQK------IKTLREKWR--ALKSDSNKYENYVNAMKQKS---QEWPGKLEKLKS----EIELKEEEIK 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  321 KYQRDIREAMAQKEdmEERITTLEKRYLSAQREstsihDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTM 400
Cdd:COG5185   348 ALQSNIDELHKQLR--KQGISTEQFELMNQERE-----KLTRELDKINIQSDKLTKSVKSRKLEAQGIFKSLEKTLRQYD 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  401 RKAETLPEVEAEL------AQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKrlsDTVDRLLT 474
Cdd:COG5185   421 SLIQNITRSRSQIghnvndSSLKINIEQLFPKGSGINESIKKSILELNDEIQERIKTEENKSITLEEDI---KNLKHDIN 497
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  475 ESNERLQLHLKERMAALEEKNVLIQESEtfrknleeslHDKERLAEEIEKLRSELDQLKM 534
Cdd:COG5185   498 ELTQILEKLELELSEANSKFELSKEENE----------RELVAQRIEIEKLEKELNDLNL 547
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
274-452 3.72e-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: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  274 QELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLikteEMNTKYQRDIREAmaqkEDMEERITTLEKRYLSaqre 353
Cdd:cd00176    64 EQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDA----DDLEQWLEEKEAALAS---- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  354 stsihdmnDKLENELANKEAILRQMEEknrqLQERLELAEQKLQQTMRKAETLPEveaelAQRIAALTKAEERHGNIEER 433
Cdd:cd00176   132 --------EDLGKDLESVEELLKKHKE----LEEELEAHEPRLKSLNELAEELLE-----EGHPDADEEIEEKLEELNER 194
                         170
                  ....*....|....*....
gi 333805618  434 MRHLEGQLEEKNQELQRAR 452
Cdd:cd00176   195 WEELLELAEERQKKLEEAL 213
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
269-480 3.89e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 41.68  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   269 QIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTlekryl 348
Cdd:pfam01576  890 RIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS------ 963
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   349 saqrestsihdmndKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRK-AETLPEVEAElaQRIAALTKAEERH 427
Cdd:pfam01576  964 --------------KYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKlKEVLLQVEDE--RRNADQYKDQAEK 1027
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333805618   428 GNIeeRMRHLEGQLEEKNQELQRAR-QREKMNEEhnkrLSDTvdrllTESNERL 480
Cdd:pfam01576 1028 GNS--RLKQLKRQLEEAEEEASRANaARRKLQRE----LDDA-----TESAEAM 1070
PRK12704 PRK12704
phosphodiesterase; Provisional
303-460 4.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  303 QEAETARKDLIKTEEmntkyqrdiREAMAQKEDMEerittlekryLSAQREstsIHDMNDKLENELANKEAILRQMEEKN 382
Cdd:PRK12704   34 KEAEEEAKRILEEAK---------KEAEAIKKEAL----------LEAKEE---IHKLRNEFEKELRERRNELQKLEKRL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  383 RQLQERLElaeqklqqtmRKAETLPEVEAELAQRIAALTKAEErhgNIEERmrhlEGQLEEK----NQELQR-------- 450
Cdd:PRK12704   92 LQKEENLD----------RKLELLEKREEELEKKEKELEQKQQ---ELEKK----EEELEELieeqLQELERisgltaee 154
                         170
                  ....*....|..
gi 333805618  451 ARQR--EKMNEE 460
Cdd:PRK12704  155 AKEIllEKVEEE 166
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
277-468 4.37e-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: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  277 LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQrDIREAMAQK----EDMEERITTLEKRYLSAQR 352
Cdd:cd07666    14 LTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMN-EYVEAFSQKinvlDKISQRIYKEQREYFEELK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  353 ESTSIHDMNDKLENELANK--------EAILRQMEEKNRQLQERLE-------LAEQKLQQTMRKAEtlpEVEAELAQRI 417
Cdd:cd07666    93 EYGPIYTLWSASEEELADSlkgmasciDRCCKATDKRMKGLSEQLLpviheyvLYSETLMGVIKRRD---QIQAELDSKV 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 333805618  418 AALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDT 468
Cdd:cd07666   170 EALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFT 220
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
386-533 5.68e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 40.04  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  386 QERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRL 465
Cdd:COG1579     6 LKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAV 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618  466 SDtvdrlltesnerlqlhLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLK 533
Cdd:COG1579    86 KD----------------ERELRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLE 137
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-682 5.83e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618    43 DRLLDTLRETQESLSLAQqrLQDVIYDRDSLQRQLnSALPQDIESLTGgLAGSKGADPPEFAALTKELNACREQLLEKE- 121
Cdd:TIGR02169  214 QALLKEKREYEGYELLKE--KEALERQKEAIERQL-ASLEEELEKLTE-EISELEKRLEEIEQLLEELNKKIKDLGEEEq 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   122 ----EEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--SGVSSEVEVLKALKSLFEHHKALDEKVRERL 195
Cdd:TIGR02169  290 lrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDL 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   196 RVSLErvsALEEELAAANQEIVALREQNVHIQRKMASSEGstesEHLEGMEPGQKVHEkRLSNGSIDSTDETSQIVELQE 275
Cdd:TIGR02169  370 RAELE---EVDKEFAETRDELKDYREKLEKLKREINELKR----ELDRLQEELQRLSE-ELADLNAAIAGIEAKINELEE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   276 LLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERIT-------------- 341
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiq 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   342 ----------TLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEK---------NRQLQERLELAEQKLQQTMRK 402
Cdd:TIGR02169  522 gvhgtvaqlgSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGF 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   403 AETLPEVEAELA-------------QRIAAltkAEERHGNIeeRMRHLEGQLEEKN---------------------QEL 448
Cdd:TIGR02169  602 AVDLVEFDPKYEpafkyvfgdtlvvEDIEA---ARRLMGKY--RMVTLEGELFEKSgamtggsraprggilfsrsepAEL 676
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   449 QRARQREKMNEEHNKRLSDTVDRLLTESNERLQL--HLKERMAALE-EKNVLIQESETFRKNLEESLHDKERLAEEIEKL 525
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQElsDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   526 RSELDQLKMRTGSLIEptiprthldTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQ 605
Cdd:TIGR02169  757 KSELKELEARIEELEE---------DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   606 IGVLSShpfESDTEMSDIDD--DDRETIFSSMDLLSPSGHSDAQTLAMM------LQEQLDAINKEIRLIQEEKESTELR 677
Cdd:TIGR02169  828 KEYLEK---EIQELQEQRIDlkEQIKSIEKEIENLNGKKEELEEELEELeaalrdLESRLGDLKKERDELEAQLRELERK 904

                   ....*
gi 333805618   678 AEEIE 682
Cdd:TIGR02169  905 IEELE 909
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
189-487 5.87e-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: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 40.87  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   189 EKVRERLRVSLERVSALEEELAAANQeivALREQNVHIQRKMASSEGSTESEHlegmEPGQKVHEKRLSNGSI-DSTDET 267
Cdd:pfam05557   44 ERESDRNQELQKRIRLLEKREAEAEE---ALREQAELNRLKKKNLEALNKKLN----EKESQLADAREVISCLkNELSEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   268 SQIVELQEL-LEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEE-------- 338
Cdd:pfam05557  117 RRQIQRQELeLSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIvknsksel 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   339 -RITTLEKRyLSAQRE-----STSIHDmNDKLENELANKEAILRQME---EKNRQLQERLELAEQKLQQ----------T 399
Cdd:pfam05557  197 aRIPELERE-LERLREhnkhlNENIEN-KLLLKEEVEDLKRKLEREEgyrEELATLELEKEKLEQELKSweklaqdtglN 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   400 MRKAETLPEVEAELAQRIAALTkaeERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLltesNER 479
Cdd:pfam05557  275 LRSPEDLSRRIEQLQQREITLK---EENSSLTSSARQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRL----QRR 347

                   ....*...
gi 333805618   480 LQLHLKER 487
Cdd:pfam05557  348 VLLLTKER 355
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
362-529 6.00e-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: 281941 [Multi-domain]  Cd Length: 218  Bit Score: 39.67  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   362 DKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRIAALTKAEERHG-----------NI 430
Cdd:pfam04012   40 GKARQALAQVIARQKQLERKLEEQKEQAKKLENKARAALTKGN--EELAREALAEIATLEKLAEALEtqltqqrsaveQL 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   431 EERMRHLEGQLEEKNQE-------LQRARQREKMNEehnkrlsdTVDRLLTESNERLQLHLKERMAALEEKNVLIQESEt 503
Cdd:pfam04012  118 RKQLAALETKIQQLKAKktalkarLKAAKAQEAVNT--------SLGSASTESATDSFERIEEKIEEREARADAAAELA- 188
                          170       180
                   ....*....|....*....|....*.
gi 333805618   504 FRKNLEESLHDKERLAEEIEKLRSEL 529
Cdd:pfam04012  189 SAQDLDAKLEAAGIQMEVSEDVLARL 214
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
903-960 6.29e-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: 6.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618  903 VVAWLElWLGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 960
Cdd:cd09487     2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
178-467 6.92e-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: 40.51  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   178 KSLFEHHKALDEKVRERLRvSLERVSALEEELAAANQEIVALREQNVH--IQRKMASSEGSTESEHLEGMEPGQKVHEKR 255
Cdd:pfam09731  121 KSEQEKEKALEEVLKEAIS-KAESATAVAKEAKDDAIQAVKAHTDSLKeaSDTAEISREKATDSALQKAEALAEKLKEVI 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   256 LSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAE-TARKDLIKTEEM---------------- 318
Cdd:pfam09731  200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElVASERIVFQQELvsifpdiipvlkednl 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   319 --NTKYQRDIREAMAQKEDMEERITTLEKR-YLSAQRESTSIHDMNDKLENELAnkEAILRQMEEKNRQLQERLELAEQK 395
Cdd:pfam09731  280 lsNDDLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDKLAEELS--ARLEEVRAADEAQLRLEFEREREE 357
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333805618   396 LQQTMRKaetlpEVEAELAQRIAALTKaeerhgnieermrHLEGQLEEKNQELQRARQR---EKMNEEHNKRLSD 467
Cdd:pfam09731  358 IRESYEE-----KLRTELERQAEAHEE-------------HLKDVLVEQEIELQREFLQdikEKVEEERAGRLLK 414
46 PHA02562
endonuclease subunit; Provisional
212-427 7.97e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  212 ANQEIVALREQNVHIQRKMAssegsTESEHLEGMEPGQKVHEKRLSNgSIDSTDET-----SQIVELQELL-------EK 279
Cdd:PHA02562  179 LNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQN-KYDELVEEaktikAEIEELTDELlnlvmdiED 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  280 QNYEMAQMKERLAALSSRVGEVEQEAE---------TARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSA 350
Cdd:PHA02562  253 PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333805618  351 QRESTSIHDMNDKLENelaNKEAILRqMEEKNRQLQERLELAEqklQQTMRKAETLPEVEAELAQRIAALTK-AEERH 427
Cdd:PHA02562  333 NEQSKKLLELKNKIST---NKQSLIT-LVDKAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSElVKEKY 403
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
1021-1065 8.71e-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  Cd Length: 69  Bit Score: 36.13  E-value: 8.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 333805618 1021 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 1065
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
RmuC COG1322
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ...
269-423 9.22e-03

DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 40.07  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  269 QIVELQELLEKQNYEMAQMKERLAALSsrvgEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKE----DMEERITTLE 344
Cdd:COG1322    22 QLLLRLGRLEQMLGELAAVLEQLLLLL----AFRAEAEQLRTFARSLQALNLELIQELNELKARLQqqllQSREQLQLLI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  345 KRYLSAQREST-SIHDMNDKLENELA--NKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEV-------EAELA 414
Cdd:COG1322    98 ESLAQLSSEFQeLANEIFEELNRRLAelNQQNLKQLLKPLREVLEKFREQLEQRIHESAEERSTLLEEidrllgeIQQLA 177

                  ....*....
gi 333805618  415 QRIAALTKA 423
Cdd:COG1322   178 QEAGNLTAA 186
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
372-541 9.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  372 EAILRQMEEKNRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRA 451
Cdd:PRK03918  138 DAILESDESREKVVRQILGLDDYE-----NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  452 RQREKmneehnkRLSDTVDRLltesnERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKErlaEEIEKLRSELDQ 531
Cdd:PRK03918  213 SSELP-------ELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE---ERIEELKKEIEE 277
                         170
                  ....*....|
gi 333805618  532 LKMRTGSLIE 541
Cdd:PRK03918  278 LEEKVKELKE 287
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
392-533 9.56e-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: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 9.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618   392 AEQKLQQTMRKAETlpeVEAELAQRIAALTKAE----ERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSD 467
Cdd:pfam02841  174 AEEVLQEFLKSKEA---VEEAILQTDQALTAKEkaieAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333805618   468 TVdrlltESNERLQLHLKERMAALEEknvliQESETFRKnleeslhdkERLAEEIEKLRSELDQLK 533
Cdd:pfam02841  251 KM-----EAEREQLLAEQERMLEHKL-----QEQEELLK---------EGFKTEAESLQKEIQDLK 297
46 PHA02562
endonuclease subunit; Provisional
294-533 9.61e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  294 LSSRVGEVEQEAET--ARKDLIKTE-EMNTKYQRDIREAMAQkedmeeRITTLEKRYLSAQRESTSIHDMNDKLENELAN 370
Cdd:PHA02562  172 NKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  371 keaILRQMEEKNRQLQE-RLELAEQKLQ-QTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQEL 448
Cdd:PHA02562  246 ---LVMDIEDPSAALNKlNTAAAKIKSKiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  449 QRARQREKMNEEHNKRLSDTvdrlltesneRLQLHLKERMAALEEKNVLIQESETfrKNLEESLHDKErlaEEIEKLRSE 528
Cdd:PHA02562  323 DELEEIMDEFNEQSKKLLEL----------KNKISTNKQSLITLVDKAKKVKAAI--EELQAEFVDNA---EELAKLQDE 387

                  ....*
gi 333805618  529 LDQLK 533
Cdd:PHA02562  388 LDKIV 392
MscK COG3264
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
273-455 9.82e-03

Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225803 [Multi-domain]  Cd Length: 835  Bit Score: 40.05  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  273 LQELLEKQ----NYEMAQMKERLAALSSRVGEVEQ-EAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRy 347
Cdd:COG3264     9 LQELLQSRrellTAESAQLEAALQLLQEAVNSKRQeEAEPAAEEAELQAELIQQELAINDQLSQALNQQTERLNALASD- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333805618  348 lsaqrestsihdmNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTmrkaETLPEVEAElaQRIAALTkaEERH 427
Cdd:COG3264    88 -------------DRQLANLLLQLLQSSRTIREQIAVLRGSLLLSRILLQQL----GPLPEAGQP--QEQFEVT--QERD 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 333805618  428 GNIEER--MRHLEGQLEEKNQELQR------ARQRE 455
Cdd:COG3264   147 ALQAEKayINALEGQAEQLTAEVRDildqilDTRRE 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
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