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Conserved domains on  [gi|1720412131|ref|XP_030109976|]
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homeobox protein cut-like 2 isoform X2 [Mus musculus]

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 ...
 1146-1222 5.90e-32

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: 119.62  E-value: 5.90e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1146 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1222
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 991-1064 9.60e-30

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: 113.46  E-value: 9.60e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412131  991 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 645-721 1.58e-27

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: 106.91  E-value: 1.58e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131  645 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 721
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1272-1328 4.01e-14

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 4.01e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1328
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-474 4.65e-09

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: 61.49  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 348
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  349 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 428
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412131  429 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 474
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 1146-1222 5.90e-32

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: 119.62  E-value: 5.90e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1146 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1222
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 991-1064 9.60e-30

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: 113.46  E-value: 9.60e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412131  991 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 645-721 1.58e-27

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: 106.91  E-value: 1.58e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131  645 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 721
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1272-1328 4.01e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 4.01e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1328
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1272-1330 3.47e-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: 59.95  E-value: 3.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412131 1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1330
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1272-1327 2.68e-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: 57.26  E-value: 2.68e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412131  1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1327
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-474 4.65e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 348
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  349 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 428
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412131  429 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 474
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 275-515 1.91e-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: 56.22  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  275 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNssIRLACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRLLKDAQQLRHSLQELEEvsanQI 430
Cdd:TIGR02168  336 AEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA----RL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  431 ADLERQLAAKSEAIEKLQEKLEAqADYEEIKTELSILRAM--KLASSTCSLPQTLAKPDDPLLVAKDVFFPTQKFLLEKP 508
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488


                   ....*..
gi 1720412131  509 ALLASPE 515
Cdd:TIGR02168  489 ARLDSLE 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-470 9.31e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 9.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  275 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKA---TQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKL 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNSSIRLAccspqgpSGE----KVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsa 427
Cdd:PRK03918   625 EEELDKAFEELAETEKRLEEL-------RKEleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK--- 694

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412131  428 nQIADLERQLAAKSEAIEKLqEKLE-AQADYEEIKTELSILRAM 470
Cdd:PRK03918   695 -TLEKLKEELEEREKAKKEL-EKLEkALERVEELREKVKKYKAL 736
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 279-459 1.54e-04

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.22  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  279 ERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:pfam05622  296 LGQEGSYRERLTeLQQLLEDANRRKNELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEA 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNSSIrlaccspQGPSGEKVSfalcsgpRLEAALASKDREIL-------RLLKDAQQLRHSLQ-ELE 423
Cdd:pfam05622  376 QSELQKKKEQIEELEPKQ-------DSNLAQKID-------ELQEALRKKDEDMKameerykKYVEKAKSVIKTLDpKQN 441

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720412131  424 EVSANQIADLERQLAAKSEAIEKLQ---EKLEAQADYEE 459
Cdd:pfam05622  442 PASPPEIQALKNQLLEKDKKIEHLErdfEKSKLQREQEE 480
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1271-1329 5.47e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 5.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412131 1271 AKKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRRE 1329
Cdd:COG5576     51 PKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
 
Name Accession Description Interval E-value
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 1146-1222 5.90e-32

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: 119.62  E-value: 5.90e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1146 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1222
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 991-1064 9.60e-30

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: 113.46  E-value: 9.60e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412131  991 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 645-721 1.58e-27

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: 106.91  E-value: 1.58e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131  645 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 721
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1272-1328 4.01e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 4.01e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131 1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1328
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1272-1330 3.47e-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: 59.95  E-value: 3.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412131 1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1330
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1272-1327 2.68e-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: 57.26  E-value: 2.68e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412131  1272 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1327
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-474 4.65e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 348
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  349 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 428
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412131  429 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 474
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-470 2.88e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQKGLQEVHITLAARLGEAEEKIKVL---HSALKATQTELLELRRKYdEEAASKADEVGLIMTNLEKANQRAE 349
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLP 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  350 AAQrEVESLREQLASVNSsiRLACCSPQGPSGEKVSFALcsgPRLEAALASKDREILRLLKD-----AQQLRHSLQELEE 424
Cdd:COG4717    130 LYQ-ELEALEAELAELPE--RLEELEERLEELRELEEEL---EELEAELAELQEELEELLEQlslatEEELQDLAEELEE 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720412131  425 VSA------NQIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAM 470
Cdd:COG4717    204 LQQrlaeleEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 273-461 4.22e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.70  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQKgLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEeaasKADEVGLIMTNLEKANQR----- 347
Cdd:COG1579     12 LQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYEEQlgnvr 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  348 ----AEAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELE 423
Cdd:COG1579     87 nnkeYEALQKEIESLKRRISDLEDEIL----------------------ELMERIEELEEELAELEAELAELEAELEEKK 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720412131  424 EVSANQIADLERQLAAKSEAIEKLQEKLEAQ--ADYEEIK 461
Cdd:COG1579    145 AELDEELAELEAELEELEAEREELAAKIPPEllALYERIR 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 275-515 1.91e-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: 56.22  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  275 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNssIRLACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRLLKDAQQLRHSLQELEEvsanQI 430
Cdd:TIGR02168  336 AEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA----RL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  431 ADLERQLAAKSEAIEKLQEKLEAqADYEEIKTELSILRAM--KLASSTCSLPQTLAKPDDPLLVAKDVFFPTQKFLLEKP 508
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488


                   ....*..
gi 1720412131  509 ALLASPE 515
Cdd:TIGR02168  489 ARLDSLE 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-468 1.98e-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: 56.22  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  265 DTLVTDTLLQKNEAERQKGLQEvhiTLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKA 344
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALR---KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  345 NQRAEAAQREVESLREQLASVNSSIRLaccspqgpsgEKVSFAlcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEE 424
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTL----------LNEEAA-----NLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720412131  425 vsanQIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELSILR 468
Cdd:TIGR02168  853 ----DIESLAAEIEELEELIEELESELEaLLNERASLEEALALLR 893
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-469 2.90e-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: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  272 LLQKNEAERQKGLQEVHIT--------LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGlimtNLEK 343
Cdd:COG1196    231 LLKLRELEAELEELEAELEeleaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  344 ANQRAEAAQREVESLREQLASVNSSIRLAccspqgpsgEKvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELE 423
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEEL---------EE---------ELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412131  424 EVSANQIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRA 469
Cdd:COG1196    369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 277-469 5.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 5.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  277 EAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVglimTNLEKANQRAEAAQREVE 356
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE----EALLEAEAELAEAEEELE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  357 SLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRhslQELEEVSANQIADLERQ 436
Cdd:COG1196    383 ELAEELLEALRAAA----------------------ELAAQLEELEEAEEALLERLERLE---EELEELEEALAELEEEE 437

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720412131  437 LAAKSEAIEKLQEKLEAQADYEEIKTELSILRA 469
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-463 5.50e-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: 54.68  E-value: 5.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAERQKGLQEVHI-TLAARLGEAEEKIKVLHSALKATQTELLELRrkydEEAASKADEVGLIMTNLEKANQRAEAAQ 352
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  353 REVESLREQLASVNSSIrlaccSPQGPSGEKVSFALCS-----------GPRLEAALASKDREILRLLKDAQQLRHSLQE 421
Cdd:TIGR02168  845 EQIEELSEDIESLAAEI-----EELEELIEELESELEAllnerasleeaLALLRSELEELSEELRELESKRSELRRELEE 919

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412131  422 LEEvsanQIADLERQLAAKSEAIEKLQEKL--EAQADYEEIKTE 463
Cdd:TIGR02168  920 LRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEAL 959
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
277-471 6.37e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  277 EAERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEvglimtnLEKANQRAEAAQREV 355
Cdd:COG4913    285 FAQRRLELLEAELEeLRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEER 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  356 ESLREQLAsvnssirlaccspqgpsgekvsfALCSgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLER 435
Cdd:COG4913    358 ERRRARLE-----------------------ALLA--ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720412131  436 QLAakseaieklqeklEAQADYEEIKTELSILRAMK 471
Cdd:COG4913    413 ALR-------------DLRRELRELEAEIASLERRK 435
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
268-470 1.90e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  268 VTDTLLQKNEAERQKGLQEVHITLAARLGEAEEKikvlhsaLKATQTELLELRRKY-----DEEAASKADEVGLIMTNLE 342
Cdd:COG3206    157 LAEAYLEQNLELRREEARKALEFLEEQLPELRKE-------LEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  343 KANQRAEAAQREVESLREQLASVNSSIRLACCSPQGPSgekvsfalcsgprLEAALASKDREILRLLK-------DAQQL 415
Cdd:COG3206    230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSArytpnhpDVIAL 296

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  416 RHSLQELEE-----------VSANQIADLERQLAAKSEAIEKLQEKL----EAQADYEEIKTELSILRAM 470
Cdd:COG3206    297 RAQIAALRAqlqqeaqrilaSLEAELEALQAREASLQAQLAQLEARLaelpELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 273-452 1.92e-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: 52.75  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQK---GLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDE---EAASKADEVGLIMTNLEKANQ 346
Cdd:TIGR02168  335 LAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLERLED 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  347 RAEAAQREVESLREQLASVNSSirlaccspqgpsgekvsfalcsgpRLEAALASKDREILRL---LKDAQQLRHSLQELE 423
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELK------------------------ELQAELEELEEELEELqeeLERLEEALEELREEL 470

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720412131  424 EVSANQIADLERQLA---AKSEAIEKLQEKLE 452
Cdd:TIGR02168  471 EEAEQALDAAERELAqlqARLDSLERLQENLE 502
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 295-476 6.32e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  295 LGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRL 371
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEelnEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  372 accspQGPSGEKVSFALCSGP------RLEA--ALASKDREILRLLKDAQ--------QLRHSLQELEEVSA---NQIAD 432
Cdd:COG3883     98 -----SGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKADKaeleakkaELEAKLAELEALKAeleAAKAE 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412131  433 LERQLAAKSEAIEKLQEKleaQADYEEIKTELSILRAMKLASST 476
Cdd:COG3883    173 LEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAA 213
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 280-469 8.84e-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: 50.84  E-value: 8.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  280 RQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEvglimtNLEKANQRAEAAQREVESLR 359
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARLSHSRIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  360 EQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAA 439
Cdd:TIGR02169  798 AELSKLEEEVS----------------------RIEARLREIEQKLNRLTLEKEYLEKEIQELQE----QRIDLKEQIKS 851

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720412131  440 KSEAIEKLQEKLEA-QADYEEIKTELSILRA 469
Cdd:TIGR02169  852 IEKEIENLNGKKEElEEELEELEAALRDLES 882
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-470 9.31e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 9.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  275 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKA---TQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKL 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNSSIRLAccspqgpSGE----KVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsa 427
Cdd:PRK03918   625 EEELDKAFEELAETEKRLEEL-------RKEleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK--- 694

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412131  428 nQIADLERQLAAKSEAIEKLqEKLE-AQADYEEIKTELSILRAM 470
Cdd:PRK03918   695 -TLEKLKEELEEREKAKKEL-EKLEkALERVEELREKVKKYKAL 736
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 274-469 1.61e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAERQKGLQEvhitlaaRLGEAE-----EKIKVLHSALKATQTELLELRR---KYDEEAASKADEVGLIMTNLEKAN 345
Cdd:TIGR02169  206 EREKAERYQALLK-------EKREYEgyellKEKEALERQKEAIERQLASLEEeleKLTEEISELEKRLEEIEQLLEELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  346 QRAEA-AQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREilrlLKDAQQLRHSLQELEE 424
Cdd:TIGR02169  279 KKIKDlGEEEQLRVKEKIGELEAEIA----------------------SLERSIAEKERE----LEDAEERLAKLEAEID 332

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720412131  425 VSANQIADLERQLAAK-------SEAIEKLQEKLEA-QADYEEIKTELSILRA 469
Cdd:TIGR02169  333 KLLAEIEELEREIEEErkrrdklTEEYAELKEELEDlRAELEEVDKEFAETRD 385
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
290-469 2.32e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  290 TLAARLGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVN 366
Cdd:COG4372     28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  367 SSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN---QIADLERQLAAKSEA 443
Cdd:COG4372    108 EEAE----------------------ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEreeELKELEEQLESLQEE 165

                          170       180
                   ....*....|....*....|....*.
gi 1720412131  444 IEKLQEKLEAQADyEEIKTELSILRA 469
Cdd:COG4372    166 LAALEQELQALSE-AEAEQALDELLK 190
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 298-471 2.87e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  298 AEEKIKVLHSALKATQTELLELRRKYDeeaaSKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSI-------- 369
Cdd:COG3883     14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerreelg 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  370 -RLACCSPQGPSGEKVSFALCSGP------RLEA--ALASKDREILRLLKDAQQlrhSLQELEEVSANQIADLERQLAAK 440
Cdd:COG3883     90 eRARALYRSGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKADKA---ELEAKKAELEAKLAELEALKAEL 166

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720412131  441 SEAIEKLQEKL-EAQADYEEIKTELSILRAMK 471
Cdd:COG3883    167 EAAKAELEAQQaEQEALLAQLSAEEAAAEAQL 198
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
294-453 3.27e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  294 RLGEAEEKIKVLhsalkatqTELLELRRKYDEEAASKADEVGLI-MTNLEKANQRAEAAQREVESLREQLASVNSSIRla 372
Cdd:COG4913    243 ALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAELEELRAELARLEAELE-- 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  373 ccspqgpsgekvsfalcsgpRLEAALASKDREILRLLkdAQQLRHSLQELEEVsANQIADLERQLAAKSEAIEKLQEKLE 452
Cdd:COG4913    313 --------------------RLEARLDALREELDELE--AQIRGNGGDRLEQL-EREIERLERELEERERRRARLEALLA 369


                   .
gi 1720412131  453 A 453
Cdd:COG4913    370 A 370
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 291-485 5.34e-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: 47.45  E-value: 5.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  291 LAARLGEAEEKIKVLHSALKATQTE---LLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNS 367
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  368 SI--RLAccspqgpsgekVSFALCSGPRLEAALASKD-----------REILRLLKD-AQQLRHSLQELEEVSA---NQI 430
Cdd:COG4942    105 ELaeLLR-----------ALYRLGRQPPLALLLSPEDfldavrrlqylKYLAPARREqAEELRADLAELAALRAeleAER 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412131  431 ADLERQLAAKSEAIEKLQEKLEAQADY-EEIKTELSILRAM--KLASSTCSLPQTLAK 485
Cdd:COG4942    174 AELEALLAELEEERAALEALKAERQKLlARLEKELAELAAElaELQQEAEELEALIAR 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-468 5.63e-05

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: 48.13  E-value: 5.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  297 EAEEKIKVLHSALKATQTELLELRRKYDEeaaskadevglIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLAccsp 376
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEE-----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQL---- 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  377 qgpsGEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKL-EAQA 455
Cdd:TIGR02168  746 ----EERIA-------QLSKELTELEAEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALdELRA 810

                          170
                   ....*....|...
gi 1720412131  456 DYEEIKTELSILR 468
Cdd:TIGR02168  811 ELTLLNEEAANLR 823
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
328-465 6.38e-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: 6.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  328 ASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNssiRLaccspqgpsgEKVSFALCSGPRLEAALASKDREILR 407
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ---RL----------AEYSWDEIDVASAEREIAELEAELER 679

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412131  408 LLKDAQQLRHSLQELEEVSAnQIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELS 465
Cdd:COG4913    680 LDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEqAEEELDELQDRLE 737
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 297-469 8.48e-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: 47.32  E-value: 8.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  297 EAEEKIKVLHSALKATQTELLELRRKYD--------EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSs 368
Cdd:TIGR04523  278 QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES- 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  369 irlaccspqgpsgEKVSfalcsgprLEAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKSEAIEKLQ 448
Cdd:TIGR04523  357 -------------ENSE--------KQRELEEKQNEIEKLKKENQSYKQEIKNLE----SQINDLESKIQNQEKLNQQKD 411

                          170       180
                   ....*....|....*....|..
gi 1720412131  449 EKLE-AQADYEEIKTELSILRA 469
Cdd:TIGR04523  412 EQIKkLQQEKELLEKEIERLKE 433
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
294-472 1.52e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  294 RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlAC 373
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  374 CSPQGPSGEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLE- 452
Cdd:COG4372     93 QAELAQAQEELE-------SLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREEELKELEEQLEs 161

                          170       180
                   ....*....|....*....|
gi 1720412131  453 AQADYEEIKTELSILRAMKL 472
Cdd:COG4372    162 LQEELAALEQELQALSEAEA 181
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 279-459 1.54e-04

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.22  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  279 ERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:pfam05622  296 LGQEGSYRERLTeLQQLLEDANRRKNELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEA 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNSSIrlaccspQGPSGEKVSfalcsgpRLEAALASKDREIL-------RLLKDAQQLRHSLQ-ELE 423
Cdd:pfam05622  376 QSELQKKKEQIEELEPKQ-------DSNLAQKID-------ELQEALRKKDEDMKameerykKYVEKAKSVIKTLDpKQN 441

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720412131  424 EVSANQIADLERQLAAKSEAIEKLQ---EKLEAQADYEE 459
Cdd:pfam05622  442 PASPPEIQALKNQLLEKDKKIEHLErdfEKSKLQREQEE 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 273-456 2.87e-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: 45.82  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQKGLQ----EVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEeAASKADEVGLIMTNLEKanqR 347
Cdd:TIGR02168  207 RQAEKAERYKELKaelrELELALLVlRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEE---E 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  348 AEAAQREVESLREQLASVNSSIRLAccspqgpsGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEVSA 427
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  428 NQ-------------------------------IADLERQLAAKSEAIEKLQEKLEAQAD 456
Cdd:TIGR02168  355 SLeaeleeleaeleelesrleeleeqletlrskVAQLELQIASLNNEIERLEARLERLED 414
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-455 2.88e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQKGLQEVHiTLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKA---DEVGLIMTNLEKANQR-- 347
Cdd:COG4942     43 LAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkEELAELLRALYRLGRQpp 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  348 -----------------------AEAAQREVESLREQLASVNSSIRLAccspqgpSGEKVSFAlcsgpRLEAALASKDRE 404
Cdd:COG4942    122 lalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAEL-------EAERAELE-----ALLAELEEERAA 189

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720412131  405 ILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQA 455
Cdd:COG4942    190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-365 3.12e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  274 QKNEAERQ-KGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQ 352
Cdd:COG4913    339 RLEQLEREiERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                           90
                   ....*....|...
gi 1720412131  353 REVESLREQLASV 365
Cdd:COG4913    419 RELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-456 3.31e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  278 AERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRR------------KYDEEAASKADEVGLIMTN---LE 342
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASsddLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  343 KANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALAskdrEILRLLKDAQQLRHSLQEL 422
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELE----QAEEELDELQDRLEAAEDL 742

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720412131  423 EEVSANQIADLERQLAAKSEAIEKLQEKLEAQAD 456
Cdd:COG4913    743 ARLELRALLEERFAAALGDAVERELRENLEERID 776
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
289-493 3.77e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  289 ITLAARLGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTN----------LEKANQRAEAAQR-- 353
Cdd:COG3206    208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalrAQLGSGPDALPELLQSpviqqlraqlAELEAELAELSARyt 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  354 ----EVESLREQLASVNSSIRLaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN- 428
Cdd:COG3206    288 pnhpDVIALRAQIAALRAQLQQ---------------------EAQRILASLEAELEALQAREASLQAQLAQLEARLAEl 346

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412131  429 -----QIADLERQLAAKSEAIEKLQEKLEaqadyeeiktELSILRAMKLAS----STCSLPQTLAKPDDPLLVA 493
Cdd:COG3206    347 peleaELRRLEREVEVARELYESLLQRLE----------EARLAEALTVGNvrviDPAVVPLKPVSPKKLLILA 410
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 273-455 5.03e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQkGLQEVHITLAARLGEAEEKIKVLHSALKAT-------QTELLELRRKYDE-----------------EAA 328
Cdd:pfam10174  298 LSKKESELL-ALQTKLETLTNQNSDCKQHIEVLKESLTAKeqraailQTEVDALRLRLEEkesflnkktkqlqdlteEKS 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  329 SKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVN---SSIRLACCSPQGPSGEKVSfALCSgprLEAALASKDREI 405
Cdd:pfam10174  377 TLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDT-ALTT---LEEALSEKERII 452

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412131  406 LRL-----------LKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLEAQA 455
Cdd:pfam10174  453 ERLkeqreredrerLEELESLKKENKDLKE----KVSALQPELTEKESSLIDLKEHASSLA 509
PRK12704 PRK12704
phosphodiesterase; Provisional
 295-459 6.70e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  295 LGEAEEKIKVL-HSALKATQTELLELRRKYDEEAASKADEVglimTNLEKANQraeaaQREvESLREQLASVNssirlac 373
Cdd:PRK12704    44 LEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLL-----QKE-ENLDRKLELLE------- 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  374 cspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRhslQELEEVSANQIADLER-----QLAAKSEAIEKLQ 448
Cdd:PRK12704   107 -------------------KREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERisgltAEEAKEILLEKVE 164

                          170
                   ....*....|....*.
gi 1720412131  449 EKLEAQA-----DYEE 459
Cdd:PRK12704   165 EEARHEAavlikEIEE 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
290-459 1.38e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  290 TLAARLGEAEEKIKVLHSALKATQTELLELRRKydEEAASKADEVGlimtnleKANQRAEAAQREVESLREQLASV-NSS 368
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYS-------WDEIDVASAEREIAELEAELERLdASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  369 IRLAccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKSEAIEKLQ 448
Cdd:COG4913    685 DDLA--------------------ALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAE 740

                          170
                   ....*....|...
gi 1720412131  449 E--KLEAQADYEE 459
Cdd:COG4913    741 DlaRLELRALLEE 753
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
277-450 1.45e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  277 EAERQKGLQEVHITLAARLGEAEEKIKVLhSALKATQTELLELRRKYDEEAASKADEVGLIMTNLE---------KANQR 347
Cdd:COG4717    318 EEELEELLAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelraalEQAEE 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  348 AEAAQREVESLREQLASVNSSIRLAccsPQGPSGEKVSFALcsgPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsA 427
Cdd:COG4717    397 YQELKEELEELEEQLEELLGELEEL---LEALDEEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEE--D 468

                          170       180
                   ....*....|....*....|...
gi 1720412131  428 NQIADLERQLAAKSEAIEKLQEK 450
Cdd:COG4717    469 GELAELLQELEELKAELRELAEE 491
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 316-463 1.98e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 40.38  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  316 LLELRRKYDEEAAskadevglimTNLEKANQRAEAAQREVESLREQL----ASVNSSIRlaccspQGPSGekvsfalcsg 391
Cdd:TIGR02473    7 LLDLREKEEEQAK----------LELAKAQAEFERLETQLQQLIKYReeyeQQALEKVG------AGTSA---------- 60

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412131  392 prleAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKS---EAIEKLQEKLEAQADYEEIKTE 463
Cdd:TIGR02473   61 ----LELSNYQRFIRQLDQRIQQQQQELALLQ----QEVEAKRERLLEARrelKALEKLKEKKQKEYRAEEAKRE 127
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
291-469 2.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  291 LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEaaSKADEVGLIMTNLEKAN-QRAEAAQREVESLREQLASVNSSI 369
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEI 541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  370 R-LACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRL-LKDAQQLRHSLQELEEV--SANQIADLERQLAAKSEAI 444
Cdd:PRK03918   542 KsLKKELEKLEELKKKLAELEKKLDeLEEELAELLKELEELgFESVEELEERLKELEPFynEYLELKDAEKELEREEKEL 621

                          170       180
                   ....*....|....*....|....*.
gi 1720412131  445 EKLQEKL-EAQADYEEIKTELSILRA 469
Cdd:PRK03918   622 KKLEEELdKAFEELAETEKRLEELRK 647
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
307-469 2.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  307 SALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLAsvnssirlaccspqgpsgekvsf 386
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE----------------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  387 alcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLEA-QADYEEIKTELS 465
Cdd:COG4372     63 ------QLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQEELEElQKERQDLEQQRK 132


                   ....
gi 1720412131  466 ILRA 469
Cdd:COG4372    133 QLEA 136
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
275-468 3.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  275 KNEAERqkgLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRK---YDEEAASKADEVGLIMTNLEKANQRAEAA 351
Cdd:PRK02224   341 NEEAES---LREDADDLEERAEELREEAAELESELEEAREAVEDRREEieeLEEEIEELRERFGDAPVDLGNAEDFLEEL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  352 QREVESLREQLASVNSSIRlaccspqgpsgeKVSFALCSGPRLEAAlaSKDREILRLLKDAQQLrHSLQELEEvsanQIA 431
Cdd:PRK02224   418 REERDELREREAELEATLR------------TARERVEEAEALLEA--GKCPECGQPVEGSPHV-ETIEEDRE----RVE 478

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720412131  432 DLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILR 468
Cdd:PRK02224   479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE 515
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 393-469 3.62e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 3.62e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412131  393 RLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQeklEAQADYEEIKTELSILRA 469
Cdd:pfam07926    5 SLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQ---ALREELNELKAEIAELKA 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-447 3.68e-03

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: 41.97  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  278 AERQKGLQEVHITLAARLGEAEEKIKVLHSALKatqtELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVES 357
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  358 LREQLASVNSSI-----RLACCSPQGPSGEKVSF--ALCSGPRLEAALASKDREILRLLKDAQQL----RHSLQELEEVS 426
Cdd:TIGR02168  920 LREKLAQLELRLeglevRIDNLQERLSEEYSLTLeeAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELK 999

                          170       180
                   ....*....|....*....|....*..
gi 1720412131  427 ------ANQIADLERQLAAKSEAIEKL 447
Cdd:TIGR02168 1000 erydflTAQKEDLTEAKETLEEAIEEI 1026
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 336-494 4.07e-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: 41.29  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  336 LIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpsgekvsfalcsgprleAALASKDREILRLLKDAQQL 415
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKEL--------------------------AALKKEEKALLKQLAALERR 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  416 RHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQadyeeiKTELS-ILRAMKLASSTcSLPQTLAKPDDPLLVAK 494
Cdd:COG4942     64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ------KEELAeLLRALYRLGRQ-PPLALLLSPEDFLDAVR 136
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 297-529 4.38e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  297 EAEEKIKVLHSALKATQtellelrrkydEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLasvnssIRLaccsp 376
Cdd:pfam12128  601 ELRERLDKAEEALQSAR-----------EKQAAAEEQLVQANGELEKASREETFARTALKNARLDL------RRL----- 658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  377 qgpSGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQ---------------IADLERQLAAKS 441
Cdd:pfam12128  659 ---FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkreartekqaywqvvEGALDAQLALLK 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  442 EAIEKLQEKLEAQADY--EEIKTELSIL-----RAMKLASSTCSLPQTL--AKPDDPLLVAKDVFFPTQkFLLEKPALLA 512
Cdd:pfam12128  736 AAIAARRSGAKAELKAleTWYKRDLASLgvdpdVIAKLKREIRTLERKIerIAVRRQEVLRYFDWYQET-WLQRRPRLAT 814

                          250
                   ....*....|....*..
gi 1720412131  513 SPEEDPSEDDSIKGSLG 529
Cdd:pfam12128  815 QLSNIERAISELQQQLA 831
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 264-464 4.70e-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: 41.96  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  264 EDTLvtdTLLQKNEAERQKglqevhitLAARLGEAEEKIkvlhsaLKATQTELLELRRKYDEEAASKADEVGLIMTNLEK 343
Cdd:TIGR00606  268 DNEI---KALKSRKKQMEK--------DNSELELKMEKV------FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEK 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  344 ANQ-RAEAAQREVESLREQlasvnSSIRLACCSPQGPSGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQEL 422
Cdd:TIGR00606  331 LNKeRRLLNQEKTELLVEQ-----GRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQED 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720412131  423 EEVSANQ-IADLERQLAAKSEAIEKLQEKLEAQADYEEIKTEL 464
Cdd:TIGR00606  406 EAKTAAQlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
292-463 5.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  292 AARLGEAEEKIKVLHSALKATQTELLELRRKYD--EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNssi 369
Cdd:PRK02224   467 VETIEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR--- 543

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  370 rlaccspqgpsgEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEV--SANQIADLERQLAAKSEAIEKL 447
Cdd:PRK02224   544 ------------ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADAEDEIERL 611

                          170
                   ....*....|....*.
gi 1720412131  448 QEKLEAQADYEEIKTE 463
Cdd:PRK02224   612 REKREALAELNDERRE 627
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 393-454 5.28e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 39.80  E-value: 5.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412131  393 RLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQ 454
Cdd:pfam06785  101 RLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQ 162
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1271-1329 5.47e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 5.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412131 1271 AKKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRRE 1329
Cdd:COG5576     51 PKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 402-469 5.50e-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: 5.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412131  402 DREILRLLKDAQQLRHSLQELEEVSAN---QIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELSILRA 469
Cdd:COG1579      2 MPEDLRALLDLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELEdLEKEIKRLELEIEEVEA 73
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
291-469 5.56e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  291 LAARLGEAEEKIKVLHSALKATQTELLELRRkydeeaaskadEVGLIMTNLEKANQRAEAAQREVESLREQLasvnssir 370
Cdd:COG1842     14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQ-----------ALAQVIANQKRLERQLEELEAEAEKWEEKA-------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  371 laccspqgpsgekvsfalcsgprlEAALaSKDREilRLLKDAQQLRHSLQeleevsaNQIADLERQLAAKSEAIEKLQEK 450
Cdd:COG1842     75 ------------------------RLAL-EKGRE--DLAREALERKAELE-------AQAEALEAQLAQLEEQVEKLKEA 120

                          170       180
                   ....*....|....*....|
gi 1720412131  451 L-EAQADYEEIKTELSILRA 469
Cdd:COG1842    121 LrQLESKLEELKAKKDTLKA 140
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 273-502 6.64e-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: 41.21  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  273 LQKNEAERQKGLQEvhitLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAAskadEVGLIMTNLEKANQRAEAAQ 352
Cdd:TIGR02169  845 LKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLRELERKIEELEAQIEKKR 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  353 REVESLREQLASVNSsiRLACCSPQGPSGEKVSFALCSGPRLEAALASKDREIlrllkdaqqlrhslQELEEVSANQIAD 432
Cdd:TIGR02169  917 KRLSELKAKLEALEE--ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI--------------RALEPVNMLAIQE 980

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  433 LERQLAAKSEAIEKlQEKLEAQ--------ADYEEIKTEL------SILRAMK-----LASSTCSLpqTLAKPDDPL--- 490
Cdd:TIGR02169  981 YEEVLKRLDELKEK-RAKLEEErkaileriEEYEKKKREVfmeafeAINENFNeifaeLSGGTGEL--ILENPDDPFagg 1057

                          250
                   ....*....|....
gi 1720412131  491 --LVAKDVFFPTQK 502
Cdd:TIGR02169 1058 leLSAKPKGKPVQR 1071
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
276-471 7.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  276 NEAERQKGLQEvhitlaARLGEAEEKIKVLHSALKATQTELLELRRKYDE--EAASKADEVGLIMTNLEKANQRAEAAQR 353
Cdd:PRK03918   241 EELEKELESLE------GSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEK 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412131  354 EVESLREQLASVNSSIrlaccspqgpsgEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSA--NQIA 431
Cdd:PRK03918   315 RLSRLEEEINGIEERI------------KELE-------EKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkEELE 375

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720412131  432 DLERQLAAKSeaIEKLQEKLE-AQADYEEIKTELSILRAMK 471
Cdd:PRK03918   376 RLKKRLTGLT--PEKLEKELEeLEKAKEEIEEEISKITARI 414
 
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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