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Conserved domains on  [gi|116517292|ref|NP_056082|]
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homeobox protein cut-like 2 isoform 1 [Homo sapiens]

Protein Classification

CUT and homeodomain domain-containing protein( domain architecture ID 11131078)

CUT and homeodomain domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 1043-1119 2.45e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 117.69  E-value: 2.45e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1043 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1119
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 892-965 4.39e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.53  E-value: 4.39e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116517292   892 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 965
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 553-625 3.89e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.06  E-value: 3.89e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116517292   553 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 625
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1169-1225 2.12e-14

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.68  E-value: 2.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1225
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-379 1.28e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  179 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 253
Cdd:COG1196   208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  254 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 333
Cdd:COG1196   277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116517292  334 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 379
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
17-269 2.36e-03

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   17 LRRLQKELNSV-ASELSARQEESEHSHKHLIELRREFKkNVPEEIREmvapvLKSFQAEVVALSKRSQEAEAAFLSVYKQ 95
Cdd:PRK03918  505 LKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKELEK-----LEELKKKLAELEKKLDELEEELAELLKE 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   96 LIEAPdpvpvFEAARSLDDRLQppsfdpsgqprrDLHTSWKRNPELL-SPKEQREgtspagptltegsrlpgipgkallt 174
Cdd:PRK03918  579 LEELG-----FESVEELEERLK------------ELEPFYNEYLELKdAEKELER------------------------- 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  175 etllqrnEAEKQKGLQEvqitlaaRLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVgliMTNLEKANQRAE 254
Cdd:PRK03918  617 -------EEKELKKLEE-------ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE---YLELSRELAGLR 679

                         250
                  ....*....|....*
gi 116517292  255 AAQREVESLREQLAS 269
Cdd:PRK03918  680 AELEELEKRREEIKK 694
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 1043-1119 2.45e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 117.69  E-value: 2.45e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1043 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1119
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 892-965 4.39e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.53  E-value: 4.39e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116517292   892 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 965
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 553-625 3.89e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.06  E-value: 3.89e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116517292   553 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 625
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1169-1225 2.12e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.68  E-value: 2.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1225
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1169-1227 1.99e-11

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 60.33  E-value: 1.99e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116517292 1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1227
Cdd:cd00086     1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1169-1224 1.42e-10

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 58.03  E-value: 1.42e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 116517292   1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1224
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-379 1.28e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  179 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 253
Cdd:COG1196   208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  254 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 333
Cdd:COG1196   277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116517292  334 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 379
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-370 4.18e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   173 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 251
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   252 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 331
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 116517292   332 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 370
Cdd:TIGR02168  909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 138-364 6.67e-06

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 50.46  E-value: 6.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   138 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 207
Cdd:pfam05622  241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   208 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 281
Cdd:pfam05622  321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   282 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 353
Cdd:pfam05622  394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466

                          250
                   ....*....|....
gi 116517292   354 ---EKLQAQSDYEE 364
Cdd:pfam05622  467 rdfEKSKLQREQEE 480
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
182-375 2.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  182 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 258
Cdd:PRK03918  547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  259 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 338
Cdd:PRK03918  627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 116517292  339 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 375
Cdd:PRK03918  700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-269 2.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   17 LRRLQKELNSV-ASELSARQEESEHSHKHLIELRREFKkNVPEEIREmvapvLKSFQAEVVALSKRSQEAEAAFLSVYKQ 95
Cdd:PRK03918  505 LKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKELEK-----LEELKKKLAELEKKLDELEEELAELLKE 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   96 LIEAPdpvpvFEAARSLDDRLQppsfdpsgqprrDLHTSWKRNPELL-SPKEQREgtspagptltegsrlpgipgkallt 174
Cdd:PRK03918  579 LEELG-----FESVEELEERLK------------ELEPFYNEYLELKdAEKELER------------------------- 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  175 etllqrnEAEKQKGLQEvqitlaaRLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVgliMTNLEKANQRAE 254
Cdd:PRK03918  617 -------EEKELKKLEE-------ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE---YLELSRELAGLR 679

                         250
                  ....*....|....*
gi 116517292  255 AAQREVESLREQLAS 269
Cdd:PRK03918  680 AELEELEKRREEIKK 694
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 219-378 2.99e-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: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  219 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 289
Cdd:cd22656    94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  290 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 365
Cdd:cd22656   163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230

                         170
                  ....*....|....
gi 116517292  366 KTEL-SILKAMKLA 378
Cdd:cd22656   231 DTDLdNLLALIGPA 244
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1169-1236 4.31e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 4.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116517292 1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1236
Cdd:COG5576    52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 1043-1119 2.45e-31

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 117.69  E-value: 2.45e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1043 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1119
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 892-965 4.39e-29

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 111.53  E-value: 4.39e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116517292   892 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 965
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 553-625 3.89e-26

CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.


Pssm-ID: 460543  Cd Length: 78  Bit Score: 103.06  E-value: 3.89e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116517292   553 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 625
Cdd:pfam02376    5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1169-1225 2.12e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.68  E-value: 2.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1225
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1169-1227 1.99e-11

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 60.33  E-value: 1.99e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116517292 1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1227
Cdd:cd00086     1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1169-1224 1.42e-10

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 58.03  E-value: 1.42e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 116517292   1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1224
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-379 1.28e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  179 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 253
Cdd:COG1196   208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  254 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 333
Cdd:COG1196   277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116517292  334 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 379
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-370 4.18e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   173 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 251
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   252 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 331
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 116517292   332 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 370
Cdd:TIGR02168  909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-364 4.54e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 4.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  175 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAE 254
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  255 AAQREVESLREQLASVNssirlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQ 334
Cdd:COG1196   387 ELLEALRAAAELAAQLE--------------------------ELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         170       180       190
                  ....*....|....*....|....*....|
gi 116517292  335 IADLERQLTAKSEAIEKLEEKLQAQSDYEE 364
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLE 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 170-383 5.54e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.32  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  170 KALLTetlLQRNEAEKQKgLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKA 249
Cdd:COG1579     7 RALLD---LQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  250 NQR---------AEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHL 320
Cdd:COG1579    79 EEQlgnvrnnkeYEALQKEIESLKRRISDLEDEIL----------------------ELMERIEELEEELAELEAELAEL 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116517292  321 QSSLQELEEASANQIADLERQLTAKSEAIEKLEEKLQAQ--SDYEEIKTELSILKAMKLASSTCS 383
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKNGLAVVPVEGGACG 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-379 1.21e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  171 ALLTETLLQRNEAEKQ-KGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVglimTNLEKA 249
Cdd:COG1196   267 AELEELRLELEELELElEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  250 NQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEe 329
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALL----------------------EAEAELAEAEEELEELAEELLEALRAAAELA- 399

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 116517292  330 asaNQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 379
Cdd:COG1196   400 ---AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-371 1.44e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  189 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEvglimtnLEKANQRAEAAQREVESLREQLA 268
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  269 svnssirlaccspqgpsgdkvnfTLCSgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLERQLTAKSEA 348
Cdd:COG4913   366 -----------------------ALLA--ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 116517292  349 IEKLEEKLQA----QSDY--------EEIKTELSI 371
Cdd:COG4913   421 LRELEAEIASlerrKSNIparllalrDALAEALGL 455
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
173-372 2.56e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  173 LTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKikvlhsaLKATQAELLELRRKYDEEAASkaDEVGLIMTNLEKANQR 252
Cdd:COG3206   157 LAEAYLEQNLELRREEARKALEFLEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLS--EEAKLLLQQLSELESQ 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  253 AEAAQREVESLREQLASVNSSIRLACCSPQGPSGDKVNftlcsgPRLEAALASKDREILRLLK-------DVQHLQSSLQ 325
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI------QQLRAQLAELEAELAELSArytpnhpDVIALRAQIA 301

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 116517292  326 ELEEASANQIADLERQLTAKSEAIEKLEEKLQAQsdYEEIKTELSIL 372
Cdd:COG3206   302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQ--LAQLEARLAEL 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-374 2.83e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  177 LLQRNEAEKQKGLQEVQIT--------LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGlimtNLEK 248
Cdd:COG1196   231 LLKLRELEAELEELEAELEeleaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  249 ANQRAEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREILRLLKDVQHLQSSLQELE 328
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEEL------------------EEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 116517292  329 EASANQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKA 374
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 196-376 4.53e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  196 LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIR 275
Cdd:COG3883    21 KQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  276 LaccspQGPSGDKVNFTLCSGP------RLEA--ALASKDREILRLLKDvqhLQSSLQELEEASANQIADLERQLTAKSE 347
Cdd:COG3883    97 R-----SGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKA---DKAELEAKKAELEAKLAELEALKAELEA 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 116517292  348 AIEKLEEKL-QAQSDYEEIKTELSILKAMK 376
Cdd:COG3883   169 AKAELEAQQaEQEALLAQLSAEEAAAEAQL 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 17-361 8.70e-07

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: 53.91  E-value: 8.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292    17 LRRLQKELNSVASELSARQEESEHSHKHliELRREFKKNVpEEIREMVAPV------LKSFQAEVVALSKRSQEAEAAFL 90
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELREELE--ELQEELKEAE-EELEELTAELqeleekLEELRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292    91 SvYKQLIEAPDpvpvfEAARSLDDRLqppsfdpsgqprRDLHTSWKRNPELLSPKEQregtspagptltegsrlpgipgK 170
Cdd:TIGR02168  292 A-LANEISRLE-----QQKQILRERL------------ANLERQLEELEAQLEELES----------------------K 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   171 ALLTETLLQRNEAEKQkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDE---EAASKADEVGLIMTNLE 247
Cdd:TIGR02168  332 LDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLE 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   248 KANQRAEAAQREVESLREQLASVnssiRLACCSPQGPSGDKVNFTLCSG-PRLEAALASKDREILRLLKDVQHLQSSLQE 326
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAERELAQ 486

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 116517292   327 LeeasANQIADLERQLTAKSEAIEKLEEKLQAQSD 361
Cdd:TIGR02168  487 L----QARLDSLERLQENLEGFSEGVKALLKNQSG 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 178-420 1.63e-06

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: 53.14  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   178 LQRNEAEKQKGLQEVQI---TLAARLGEAEEKIKVLHSALKATQAEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQ 251
Cdd:TIGR02168  251 AEEELEELTAELQELEEkleELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   252 RAEAAQREVESLREQLASVNssIRLACCSPQGPSGDKVNFTLCSGPR-LEAALASKDREILRLLKDVQHLQSSLQELEEa 330
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA- 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   331 sanQIADLERQLTAKSEAIEKLEEKLQAQsDYEEIKTELSILKAM--KLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKF 408
Cdd:TIGR02168  408 ---RLERLEDRRERLQQEIEELLKKLEEA-ELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERE 483

                          250
                   ....*....|..
gi 116517292   409 LLEKPSLLASPE 420
Cdd:TIGR02168  484 LAQLQARLDSLE 495
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
179-375 3.14e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  179 QRNEAEKQKG----LQEVQITLAARLGEAEEKIKVL--HSALKATQAELLELRRKYdEEAASKADEVGLIMTNLEKANQR 252
Cdd:COG4717    79 ELKEAEEKEEeyaeLQEELEELEEELEELEAELEELreELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  253 AEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgprLEAALASKDREILRLLKDVQHLQSSLQELEEasa 332
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEEL---------------------LEQLSLATEEELQDLAEELEELQQRLAELEE--- 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 116517292  333 nQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 375
Cdd:COG4717   214 -ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
182-376 4.39e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  182 EAEKQ-KGLQEVQiTLAARLGEAEEKIKVLHSALKATQAELLELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAAQRE 259
Cdd:COG4913   246 DAREQiELLEPIR-ELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREE 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  260 VESLREQLASvNSSIRLAccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIA 336
Cdd:COG4913   325 LDELEAQIRG-NGGDRLE--------------------QLEREIERLERELEERERRRARLEALLAALGlplPASAEEFA 383

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116517292  337 DLERQLTAKSEAIEKLEEKLQ------------AQSDYEEIKTELSILKAMK 376
Cdd:COG4913   384 ALRAEAAALLEALEEELEALEealaeaeaalrdLRRELRELEAEIASLERRK 435
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 138-364 6.67e-06

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 50.46  E-value: 6.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   138 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 207
Cdd:pfam05622  241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   208 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 281
Cdd:pfam05622  321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   282 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 353
Cdd:pfam05622  394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466

                          250
                   ....*....|....
gi 116517292   354 ---EKLQAQSDYEE 364
Cdd:pfam05622  467 rdfEKSKLQREQEE 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-376 8.66e-06

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: 50.44  E-value: 8.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   184 EKQKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEeAASKADEVGLIMTNLEKanqRAEAAQREVES 262
Cdd:TIGR02168  217 ELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEE---EIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   263 LREQLASVNSSIRLAccspqgpsGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIADLE 339
Cdd:TIGR02168  293 LANEISRLEQQKQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELE 364

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 116517292   340 RQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILKAMK 376
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRS-KVAQLELQIASLNN 400
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
169-430 1.50e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  169 GKALLTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEK 248
Cdd:COG4372     9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  249 ANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE 328
Cdd:COG4372    85 LNEQLQAAQAELAQAQEELESLQEEAE----------------------ELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  329 EASAN---QIADLERQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILK--AMKLASSTCSLPQGMAKPEDSLLIAKEAFF 403
Cdd:COG4372   143 SEIAEreeELKELEEQLESLQEELAALEQELQALSE-AEAEQALDELLkeANRNAEKEEELAEAEKLIESLPRELAEELL 221

                         250       260
                  ....*....|....*....|....*..
gi 116517292  404 PTQKFLLEKPSLLASPEEDPSEDDSIK 430
Cdd:COG4372   222 EAKDSLEAKLGLALSALLDALELEEDK 248
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
182-375 2.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  182 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 258
Cdd:PRK03918  547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  259 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 338
Cdd:PRK03918  627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 116517292  339 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 375
Cdd:PRK03918  700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 183-374 3.28e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  183 AEKQKGLQEVQITLAA---RLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQRE 259
Cdd:COG4942    23 AEAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  260 VESLREQLASVnssIRLACCSPQGPsgdKVNFTLCSGPRLEAA-----LASKDREILRLLKDVQHLQSSLQELEEASANQ 334
Cdd:COG4942    99 LEAQKEELAEL---LRALYRLGRQP---PLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 116517292  335 IADLERQLTAKSEAIEKLEEKLQAQ--------SDYEEIKTELSILKA 374
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERqkllarleKELAELAAELAELQQ 220
PRK12704 PRK12704
phosphodiesterase; Provisional
 200-359 4.24e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  200 LGEAEEKIKVL-HSALKATQAELLELRRKYDEEAASKADEVglimTNLEKANQraeaaQREvESLREQLASVNssirlac 278
Cdd:PRK12704   44 LEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLL-----QKE-ENLDRKLELLE------- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  279 cspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQsslQELEEASANQIADLER--QLT---AKSEAIEKLE 353
Cdd:PRK12704  107 -------------------KREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERisGLTaeeAKEILLEKVE 164


                  ....*.
gi 116517292  354 EKLQAQ 359
Cdd:PRK12704  165 EEARHE 170
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
233-370 5.54e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  233 ASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNssiRLAccspqgpsgdKVNFTLCSGPRLEAALASKDREILR 312
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ---RLA----------EYSWDEIDVASAEREIAELEAELER 679

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116517292  313 LLK---DVQHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELS 370
Cdd:COG4913   680 LDAssdDLAALEEQLEELEA----ELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLE 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-361 1.02e-04

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: 46.97  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   202 EAEEKIKVLHSALKATQAELLELRRKYDEeaaskadevglIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLACCSP 281
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEE-----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   282 QgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN---QIADLERQLTAKSEAIEKLEEKLQA 358
Cdd:TIGR02168  750 A---------------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELTL 814


                   ...
gi 116517292   359 QSD 361
Cdd:TIGR02168  815 LNE 817
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-270 1.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  178 LQRNEAEKQKGLQEVQitlaARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQ 257
Cdd:COG4913   343 LEREIERLERELEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                          90
                  ....*....|...
gi 116517292  258 REVESLREQLASV 270
Cdd:COG4913   419 RELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
183-362 1.92e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  183 AEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRR------------KYDEEAASKADEVGLIMTN---LE 247
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASsddLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  248 KANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSS---- 323
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELEQAEEELDELQDRLEAAEDLarle 746

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 116517292  324 ---------LQELEEASANQI-ADLERQLTAKSEAIEKLEEKL-QAQSDY 362
Cdd:COG4913   747 lralleerfAAALGDAVERELrENLEERIDALRARLNRAEEELeRAMRAF 796
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 182-373 4.01e-04

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: 45.06  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   182 EAEKQKGLQEvqitlaarLGEAEEKIKVLHSALKATQAELLELRR------KYDEEAASKAD-EVGLIMTNLEKANQRAE 254
Cdd:TIGR02169  169 DRKKEKALEE--------LEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREyEGYELLKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   255 AAQREVESLREQLASVNSSIrlaccspqgpsgDKVNFTLcsgPRLEAALASKDREILRLLKDVQ-HLQSSLQELEeasaN 333
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEI------------SELEKRL---EEIEQLLEELNKKIKDLGEEEQlRVKEKIGELE----A 301

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 116517292   334 QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILK 373
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIEELE 342
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 189-431 4.04e-04

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: 45.06  E-value: 4.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   189 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKAdEVGLIMTNLEK--ANQRAEAAQREVESLREQ 266
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEArlSHSRIPEIQAELSKLEEE 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   267 LASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEasanQIADLERQ---LT 343
Cdd:TIGR02169  807 VSRIEARLR----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEienLN 860

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   344 AKSEAIEKLEEKLQAQ-----SDYEEIKTELSILKA----MKLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKFLLEKPs 414
Cdd:TIGR02169  861 GKKEELEEELEELEAAlrdleSRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP- 939

                          250
                   ....*....|....*..
gi 116517292   415 lLASPEEDPSEDDSIKD 431
Cdd:TIGR02169  940 -KGEDEEIPEEELSLED 955
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 178-372 4.51e-04

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: 45.06  E-value: 4.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   178 LQRNEAEKQKGLQEVQITLA---ARLGEAEEKIKVLH--------------SALKATQAELLELRRKYDEEAASKA---D 237
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEreieeerkrrdkltEEYAELKEELEDLRAELEEVDKEFAetrD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   238 EVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDV 317
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA----------------------DLNAAIAGIEAKINELEEEK 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 116517292   318 QHLQSSLQELE---EASANQIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSIL 372
Cdd:TIGR02169  444 EDKALEIKKQEwklEQLAADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARAS 502
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
180-373 8.61e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  180 RNEAEkqkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRK---YDEEAASKADEVGLIMTNLEKANQRAEAA 256
Cdd:PRK02224  341 NEEAE---SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEieeLEEEIEELRERFGDAPVDLGNAEDFLEEL 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  257 QREVESLREQLASVNSSIRlaccspqgpsgdKVNFTLCSGPRLEAalASKDREILRLLKDVQHLqSSLQELEEasanQIA 336
Cdd:PRK02224  418 REERDELREREAELEATLR------------TARERVEEAEALLE--AGKCPECGQPVEGSPHV-ETIEEDRE----RVE 478

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 116517292  337 DLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILK 373
Cdd:PRK02224  479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE 515
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-376 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  162 SRLPGIPGKALLTETLLQRNEAEKQKgLQEVQITLAARLGEA---EEKIKVLHSALKATQAELLELRRKYDE--EAASKA 236
Cdd:PRK03918  214 SELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKElkELKEKA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  237 DEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcSGPRLEAALASKDREILRLLKD 316
Cdd:PRK03918  293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-------------------ELEEKEERLEELKKKLKELEKR 353

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116517292  317 VQHLQSSLQELEEASA--NQIADLERQLTAKSeaIEKLEEKLQ-AQSDYEEIKTELSILKAMK 376
Cdd:PRK03918  354 LEELEERHELYEEAKAkkEELERLKKRLTGLT--PEKLEKELEeLEKAKEEIEEEISKITARI 414
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-355 1.39e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  170 KALLTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAA------------SKA 236
Cdd:COG4942    40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlGRQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  237 DEVGLIM--TNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLL 314
Cdd:COG4942   120 PPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------ELAALRAELEAERAELE 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 116517292  315 KDVQHLQSSLQELEEASANQ---IADLERQLTAKSEAIEKLEEK 355
Cdd:COG4942   178 ALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQE 221
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
17-374 1.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   17 LRRLQKELNSVASELSARQEESEHSHKHLIELRREFKKNVPEEIREMVApVLKSFQAEVVALSKRSQEAEAAFLSVYKQL 96
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEEL 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   97 IEAPDPVPVFEAARSLDDRLQPP-------SFDPSGqprrdlhtswkrnPELLSPKEQREGTSPAGPTLTEGSRLPGIPG 169
Cdd:COG4717   230 EQLENELEAAALEERLKEARLLLliaaallALLGLG-------------GSLLSLILTIAGVLFLVLGLLALLFLLLARE 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  170 KALLTETLLQRNEAEKQKGLQEVQIT-LAARLG--------EAEEKIKVLhSALKATQAELLELRRKYDEEAASKADEVG 240
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEeLLAALGlppdlspeELLELLDRI-EELQELLREAEELEEELQLEELEQEIAAL 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  241 LI---MTNLEKANQRAEAAQREVEsLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREilRLLKDV 317
Cdd:COG4717   376 LAeagVEDEEELRAALEQAEEYQE-LKEELEELEEQLEEL------------------LGELEELLEALDEE--ELEEEL 434

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116517292  318 QHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEklqaQSDYEEIKTELSILKA 374
Cdd:COG4717   435 EELEEELEELEE----ELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-369 1.61e-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: 43.13  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292    16 DLRRLQKELNSVASELSARQEESEHSHKHLIELRREFKKNVpeEIREMVAPVLKSFQAEVVALsKRSQEAEAAFLSVYKQ 95
Cdd:TIGR02169  696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK--ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292    96 LIEApdpvpVFEAARSLDDRLQPPSFDPSGQPRRDLHTSWKRNPELLSPKEQREGTSPAGPTLTEGSRlpgipgkallTE 175
Cdd:TIGR02169  773 DLHK-----LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI----------QE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   176 TLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKA---DEVGLIMTNLEKANQ 251
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIeNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLReleRKIEELEAQIEKKRK 917

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   252 RAEAAQREVESLREQLASvnssirlaccspqgpsgdkvnftlcsgprLEAALASkDREILRLLKDVQHLQSSLQELEEAs 331
Cdd:TIGR02169  918 RLSELKAKLEALEEELSE-----------------------------IEDPKGE-DEEIPEEELSLEDVQAELQRVEEE- 966

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 116517292   332 anqIADLErqlTAKSEAIEKLEEKLQAQSDYEEIKTEL 369
Cdd:TIGR02169  967 ---IRALE---PVNMLAIQEYEEVLKRLDELKEKRAKL 998
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 189-359 1.87e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  189 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAAS------KADEVGLIM--TNLEKANQRAEAAQREV 260
Cdd:COG3883    49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsggSVSYLDVLLgsESFSDFLDRLSALSKIA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  261 ESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgPRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLER 340
Cdd:COG3883   129 DADADLLEELKADKAEL-------------------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189

                         170
                  ....*....|....*....
gi 116517292  341 QLTAKSEAIEKLEEKLQAQ 359
Cdd:COG3883   190 EEAAAEAQLAELEAELAAA 208
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-269 2.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   17 LRRLQKELNSV-ASELSARQEESEHSHKHLIELRREFKkNVPEEIREmvapvLKSFQAEVVALSKRSQEAEAAFLSVYKQ 95
Cdd:PRK03918  505 LKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKELEK-----LEELKKKLAELEKKLDELEEELAELLKE 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   96 LIEAPdpvpvFEAARSLDDRLQppsfdpsgqprrDLHTSWKRNPELL-SPKEQREgtspagptltegsrlpgipgkallt 174
Cdd:PRK03918  579 LEELG-----FESVEELEERLK------------ELEPFYNEYLELKdAEKELER------------------------- 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  175 etllqrnEAEKQKGLQEvqitlaaRLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVgliMTNLEKANQRAE 254
Cdd:PRK03918  617 -------EEKELKKLEE-------ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE---YLELSRELAGLR 679

                         250
                  ....*....|....*
gi 116517292  255 AAQREVESLREQLAS 269
Cdd:PRK03918  680 AELEELEKRREEIKK 694
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 179-358 2.86e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.13  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   179 QRNEAEKQKGLQEVQITLA--ARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNL--EKANQRAE 254
Cdd:pfam12795    9 KLDEAAKKKLLQDLQQALSllDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLslEELEQRLL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   255 AAQREVESLREQLASVNSSIRLACCSPQGPSG---------DKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQ 325
Cdd:pfam12795   89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQqlsearqrlQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDML 168

                          170       180       190
                   ....*....|....*....|....*....|....
gi 116517292   326 ELEEASANQIADLER-QLTAKSEAIEKLEEKLQA 358
Cdd:pfam12795  169 EQELLSNNNRQDLLKaRRDLLTLRIQRLEQQLQA 202
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 219-378 2.99e-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: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  219 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 289
Cdd:cd22656    94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  290 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 365
Cdd:cd22656   163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230

                         170
                  ....*....|....
gi 116517292  366 KTEL-SILKAMKLA 378
Cdd:cd22656   231 DTDLdNLLALIGPA 244
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1169-1236 4.31e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 4.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116517292 1169 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1236
Cdd:COG5576    52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 307-374 5.47e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 5.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116517292  307 DREILRLLKDVQHLQSSLQELEEASAN---QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILKA 374
Cdd:COG1579     2 MPEDLRALLDLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELeDLEKEIKRLELEIEEVEA 73
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-374 6.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   16 DLRRLQKELNSVASELSARQEESEHSHKHLIELRR---EFKKNVP--EEIREMVAPvLKSFQAEVVALSKRSQEAEAAFL 90
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleELEERHElyEEAKAKKEE-LERLKKRLTGLTPEKLEKELEEL 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   91 SVYKQLIEapdpvpvfEAARSLDDRlqppsfdpsgqpRRDLHTSWKRNPELLSPKEQREGTSPA-GPTLTEGSRlpgipg 169
Cdd:PRK03918  397 EKAKEEIE--------EEISKITAR------------IGELKKEIKELKKAIEELKKAKGKCPVcGRELTEEHR------ 450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  170 KALLTETLLQRNEAEKQKglqevqITLAARLGEAEEKIKVLHSALKaTQAELLELRRKYDE--EAASKADEVGLimTNLE 247
Cdd:PRK03918  451 KELLEEYTAELKRIEKEL------KEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQlkELEEKLKKYNL--EELE 521

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292  248 KANQRAEAAQREVESLREQLASVNSSIRLAccSPQGPSGDKVNFTLCSgprLEAALASKDREILRL-LKDVQHLQSSLQE 326
Cdd:PRK03918  522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKL--EELKKKLAELEKKLDE---LEEELAELLKELEELgFESVEELEERLKE 596

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 116517292  327 LEEA--SANQIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILKA 374
Cdd:PRK03918  597 LEPFynEYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKRLEELRK 647
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 175-269 9.11e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116517292   175 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevgliMTNLEKANQRae 254
Cdd:pfam01576  480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT--------LEALEEGKKR-- 549

                           90
                   ....*....|....*
gi 116517292   255 aAQREVESLREQLAS 269
Cdd:pfam01576  550 -LQRELEALTQQLEE 563
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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