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Conserved domains on  [gi|1720412145|ref|XP_030109978|]
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homeobox protein cut-like 2 isoform X7 [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 ...
 988-1064 6.76e-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: 119.23  E-value: 6.76e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  988 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 833-906 1.05e-29

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


:

Pssm-ID: 460543  Cd Length: 78  Bit Score: 113.07  E-value: 1.05e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412145  833 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 906
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 487-563 1.78e-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: 1.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  487 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1114-1170 3.03e-14

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 3.03e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145 1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1170
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-316 2.75e-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: 61.88  E-value: 2.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 190
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  191 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 270
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412145  271 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 316
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 ...
 988-1064 6.76e-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: 119.23  E-value: 6.76e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  988 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 833-906 1.05e-29

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


Pssm-ID: 460543  Cd Length: 78  Bit Score: 113.07  E-value: 1.05e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412145  833 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 906
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 487-563 1.78e-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: 1.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  487 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1114-1170 3.03e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 3.03e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145 1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1170
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1114-1172 2.91e-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: 2.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412145 1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1172
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1114-1169 2.12e-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: 57.65  E-value: 2.12e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412145  1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1169
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-316 2.75e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 190
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  191 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 270
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412145  271 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 316
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-357 1.58e-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: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  117 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNssIRLACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRLLKDAQQLRHSLQELEEvsanQI 272
Cdd:TIGR02168  336 AEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA----RL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  273 ADLERQLAAKSEAIEKLQEKLEAqADYEEIKTELSILRAM--KLASSTCSLPQTLAKPDDPLLVAKDVFFPTQKFLLEKP 350
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488


                   ....*..
gi 1720412145  351 ALLASPE 357
Cdd:TIGR02168  489 ARLDSLE 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-312 8.46e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  117 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKA---TQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKL 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNSSIRLAccspqgpSGE----KVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsa 269
Cdd:PRK03918   625 EEELDKAFEELAETEKRLEEL-------RKEleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK--- 694

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412145  270 nQIADLERQLAAKSEAIEKLqEKLE-AQADYEEIKTELSILRAM 312
Cdd:PRK03918   695 -TLEKLKEELEEREKAKKEL-EKLEkALERVEELREKVKKYKAL 736
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 121-301 1.66e-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: 45.84  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  121 ERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:pfam05622  296 LGQEGSYRERLTeLQQLLEDANRRKNELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEA 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNSSIrlaccspQGPSGEKVSfalcsgpRLEAALASKDREIL-------RLLKDAQQLRHSLQ-ELE 265
Cdd:pfam05622  376 QSELQKKKEQIEELEPKQ-------DSNLAQKID-------ELQEALRKKDEDMKameerykKYVEKAKSVIKTLDpKQN 441

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720412145  266 EVSANQIADLERQLAAKSEAIEKLQ---EKLEAQADYEE 301
Cdd:pfam05622  442 PASPPEIQALKNQLLEKDKKIEHLErdfEKSKLQREQEE 480
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1113-1171 4.85e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 4.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412145 1113 AKKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRRE 1171
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 ...
 988-1064 6.76e-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: 119.23  E-value: 6.76e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  988 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLSDPHNVEKL 1064
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 833-906 1.05e-29

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


Pssm-ID: 460543  Cd Length: 78  Bit Score: 113.07  E-value: 1.05e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412145  833 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 906
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
CUT pfam02376
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ...
 487-563 1.78e-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: 1.78e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  487 EEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376    1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
Homeodomain pfam00046
Homeodomain;
1114-1170 3.03e-14

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 68.30  E-value: 3.03e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145 1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1170
Cdd:pfam00046    1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 1114-1172 2.91e-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: 2.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412145 1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1172
Cdd:cd00086      1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 1114-1169 2.12e-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: 57.65  E-value: 2.12e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412145  1114 KKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1169
Cdd:smart00389    2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-316 2.75e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAER----QKGLQEVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASkadevglimtnLEKANQRA 190
Cdd:COG1196    208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  191 EAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN 270
Cdd:COG1196    277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412145  271 QIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLAS 316
Cdd:COG1196    335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-312 2.50e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQKGLQEVHITLAARLGEAEEKIKVL---HSALKATQTELLELRRKYdEEAASKADEVGLIMTNLEKANQRAE 191
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLP 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  192 AAQrEVESLREQLASVNSsiRLACCSPQGPSGEKVSFALcsgPRLEAALASKDREILRLLKD-----AQQLRHSLQELEE 266
Cdd:COG4717    130 LYQ-ELEALEAELAELPE--RLEELEERLEELRELEEEL---EELEAELAELQEELEELLEQlslatEEELQDLAEELEE 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720412145  267 VSA------NQIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAM 312
Cdd:COG4717    204 LQQrlaeleEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 115-320 3.42e-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: 56.09  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQKgLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEeaasKADEVGLIMTNLEKANQR----- 189
Cdd:COG1579     12 LQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYEEQlgnvr 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  190 ----AEAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELE 265
Cdd:COG1579     87 nnkeYEALQKEIESLKRRISDLEDEIL----------------------ELMERIEELEEELAELEAELAELEAELEEKK 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  266 EVSANQIADLERQLAAKSEAIEKLQEKLEAQ--ADYEEIKTELSILRAMKLASSTCS 320
Cdd:COG1579    145 AELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKNGLAVVPVEGGACG 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-357 1.58e-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: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  117 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNssIRLACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRLLKDAQQLRHSLQELEEvsanQI 272
Cdd:TIGR02168  336 AEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA----RL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  273 ADLERQLAAKSEAIEKLQEKLEAqADYEEIKTELSILRAM--KLASSTCSLPQTLAKPDDPLLVAKDVFFPTQKFLLEKP 350
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488


                   ....*..
gi 1720412145  351 ALLASPE 357
Cdd:TIGR02168  489 ARLDSLE 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-310 1.65e-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: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  107 DTLVTDTLLQKNEAERQKGLQEvhiTLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKA 186
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALR---KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  187 NQRAEAAQREVESLREQLASVNSSIRLaccspqgpsgEKVSFAlcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEE 266
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTL----------LNEEAA-----NLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720412145  267 vsanQIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELSILR 310
Cdd:TIGR02168  853 ----DIESLAAEIEELEELIEELESELEaLLNERASLEEALALLR 893
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-311 1.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  114 LLQKNEAERQKGLQEVHIT--------LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGlimtNLEK 185
Cdd:COG1196    231 LLKLRELEAELEELEAELEeleaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  186 ANQRAEAAQREVESLREQLASVNSSIRLAccspqgpsgEKvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELE 265
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEEL---------EE---------ELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720412145  266 EVSANQIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRA 311
Cdd:COG1196    369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 119-311 3.22e-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: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  119 EAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVglimTNLEKANQRAEAAQREVE 198
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE----EALLEAEAELAEAEEELE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  199 SLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRhslQELEEVSANQIADLERQ 278
Cdd:COG1196    383 ELAEELLEALRAAA----------------------ELAAQLEELEEAEEALLERLERLE---EELEELEEALAELEEEE 437

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720412145  279 LAAKSEAIEKLQEKLEAQADYEEIKTELSILRA 311
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
119-313 3.88e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  119 EAERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEvglimtnLEKANQRAEAAQREV 197
Cdd:COG4913    285 FAQRRLELLEAELEeLRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEER 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  198 ESLREQLAsvnssirlaccspqgpsgekvsfALCSgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLER 277
Cdd:COG4913    358 ERRRARLE-----------------------ALLA--ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720412145  278 QLAakseaieklqeklEAQADYEEIKTELSILRAMK 313
Cdd:COG4913    413 ALR-------------DLRRELRELEAEIASLERRK 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 116-305 4.32e-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: 4.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAERQKGLQEVHI-TLAARLGEAEEKIKVLHSALKATQTELLELRrkydEEAASKADEVGLIMTNLEKANQRAEAAQ 194
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  195 REVESLREQLASVNSSIrlaccSPQGPSGEKVSFALCS-----------GPRLEAALASKDREILRLLKDAQQLRHSLQE 263
Cdd:TIGR02168  845 EQIEELSEDIESLAAEI-----EELEELIEELESELEAllnerasleeaLALLRSELEELSEELRELESKRSELRRELEE 919

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412145  264 LEEvsanQIADLERQLAAKSEAIEKLQEKL--EAQADYEEIKTE 305
Cdd:TIGR02168  920 LRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEAL 959
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
110-312 9.68e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.48  E-value: 9.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  110 VTDTLLQKNEAERQKGLQEVHITLAARLGEAEEKikvlhsaLKATQTELLELRRKY-----DEEAASKADEVGLIMTNLE 184
Cdd:COG3206    157 LAEAYLEQNLELRREEARKALEFLEEQLPELRKE-------LEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  185 KANQRAEAAQREVESLREQLASVNSSIRLACCSPQGPSgekvsfalcsgprLEAALASKDREILRLLK-------DAQQL 257
Cdd:COG3206    230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-------------LRAQLAELEAELAELSArytpnhpDVIAL 296

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  258 RHSLQELEE-----------VSANQIADLERQLAAKSEAIEKLQEKL----EAQADYEEIKTELSILRAM 312
Cdd:COG3206    297 RAQIAALRAqlqqeaqrilaSLEAELEALQAREASLQAQLAQLEARLaelpELEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-294 1.63e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQK---GLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDE---EAASKADEVGLIMTNLEKANQ 188
Cdd:TIGR02168  335 LAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLERLED 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  189 RAEAAQREVESLREQLASVNSSirlaccspqgpsgekvsfalcsgpRLEAALASKDREILRL---LKDAQQLRHSLQELE 265
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELK------------------------ELQAELEELEEELEELqeeLERLEEALEELREEL 470

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720412145  266 EVSANQIADLERQLA---AKSEAIEKLQEKLE 294
Cdd:TIGR02168  471 EEAEQALDAAERELAqlqARLDSLERLQENLE 502
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 137-318 3.45e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  137 LGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRL 213
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEelnEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  214 accspQGPSGEKVSFALCSGP------RLEA--ALASKDREILRLLKDAQ--------QLRHSLQELEEVSA---NQIAD 274
Cdd:COG3883     98 -----SGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKADKaeleakkaELEAKLAELEALKAeleAAKAE 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412145  275 LERQLAAKSEAIEKLQEKleaQADYEEIKTELSILRAMKLASST 318
Cdd:COG3883    173 LEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAA 213
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-311 7.45e-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: 7.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  122 RQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEvglimtNLEKANQRAEAAQREVESLR 201
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARLSHSRIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  202 EQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAA 281
Cdd:TIGR02169  798 AELSKLEEEVS----------------------RIEARLREIEQKLNRLTLEKEYLEKEIQELQE----QRIDLKEQIKS 851

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720412145  282 KSEAIEKLQEKLEA-QADYEEIKTELSILRA 311
Cdd:TIGR02169  852 IEKEIENLNGKKEElEEELEELEAALRDLES 882
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-312 8.46e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  117 KNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKA---TQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKL 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNSSIRLAccspqgpSGE----KVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsa 269
Cdd:PRK03918   625 EEELDKAFEELAETEKRLEEL-------RKEleelEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK--- 694

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1720412145  270 nQIADLERQLAAKSEAIEKLqEKLE-AQADYEEIKTELSILRAM 312
Cdd:PRK03918   695 -TLEKLKEELEEREKAKKEL-EKLEkALERVEELREKVKKYKAL 736
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 116-311 1.32e-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: 50.07  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAERQKGLQEvhitlaaRLGEAE-----EKIKVLHSALKATQTELLELRR---KYDEEAASKADEVGLIMTNLEKAN 187
Cdd:TIGR02169  206 EREKAERYQALLK-------EKREYEgyellKEKEALERQKEAIERQLASLEEeleKLTEEISELEKRLEEIEQLLEELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  188 QRAEA-AQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREilrlLKDAQQLRHSLQELEE 266
Cdd:TIGR02169  279 KKIKDlGEEEQLRVKEKIGELEAEIA----------------------SLERSIAEKERE----LEDAEERLAKLEAEID 332

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720412145  267 VSANQIADLERQLAAK-------SEAIEKLQEKLEA-QADYEEIKTELSILRA 311
Cdd:TIGR02169  333 KLLAEIEELEREIEEErkrrdklTEEYAELKEELEDlRAELEEVDKEFAETRD 385
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 140-313 1.65e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  140 AEEKIKVLHSALKATQTELLELRRKYDeeaaSKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSI-------- 211
Cdd:COG3883     14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerreelg 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  212 -RLACCSPQGPSGEKVSFALCSGP------RLEA--ALASKDREILRLLKDAQQlrhSLQELEEVSANQIADLERQLAAK 282
Cdd:COG3883     90 eRARALYRSGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKADKA---ELEAKKAELEAKLAELEALKAEL 166

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720412145  283 SEAIEKLQEKL-EAQADYEEIKTELSILRAMK 313
Cdd:COG3883    167 EAAKAELEAQQaEQEALLAQLSAEEAAAEAQL 198
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
107-295 2.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  107 DTLVTDTLLQKNEAERQ--------KGLQEVHitlaARLGEAEEKIKVLhsalkatqTELLELRRKYDEEAASKADEVGL 178
Cdd:COG4913    210 DDFVREYMLEEPDTFEAadalvehfDDLERAH----EALEDAREQIELL--------EPIRELAERYAAARERLAELEYL 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  179 I-MTNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLkdAQQL 257
Cdd:COG4913    278 RaALRLWFAQRRLELLEAELEELRAELARLEAELE----------------------RLEARLDALREELDELE--AQIR 333

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720412145  258 RHSLQELEEVsANQIADLERQLAAKSEAIEKLQEKLEA 295
Cdd:COG4913    334 GNGGDRLEQL-EREIERLERELEERERRRARLEALLAA 370
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
132-311 2.59e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  132 TLAARLGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVN 208
Cdd:COG4372     28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  209 SSIRlaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN---QIADLERQLAAKSEA 285
Cdd:COG4372    108 EEAE----------------------ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEreeELKELEEQLESLQEE 165

                          170       180
                   ....*....|....*....|....*.
gi 1720412145  286 IEKLQEKLEAQADyEEIKTELSILRA 311
Cdd:COG4372    166 LAALEQELQALSE-AEAEQALDELLK 190
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 133-327 3.18e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  133 LAARLGEAEEKIKVLHSALKATQTE---LLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNS 209
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  210 SI--RLAccspqgpsgekVSFALCSGPRLEAALASKD-----------REILRLLKD-AQQLRHSLQELEEVSA---NQI 272
Cdd:COG4942    105 ELaeLLR-----------ALYRLGRQPPLALLLSPEDfldavrrlqylKYLAPARREqAEELRADLAELAALRAeleAER 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412145  273 ADLERQLAAKSEAIEKLQEKLEAQADY-EEIKTELSILRAM--KLASSTCSLPQTLAK 327
Cdd:COG4942    174 AELEALLAELEEERAALEALKAERQKLlARLEKELAELAAElaELQQEAEELEALIAR 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-307 4.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  170 ASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNssiRLaccspqgpsgEKVSFALCSGPRLEAALASKDREILR 249
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ---RL----------AEYSWDEIDVASAEREIAELEAELER 679

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412145  250 LLKDAQQLRHSLQELEEVSAnQIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELS 307
Cdd:COG4913    680 LDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEqAEEELDELQDRLE 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-310 4.79e-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: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  139 EAEEKIKVLHSALKATQTELLELRRKYDEeaaskadevglIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLAccsp 218
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEE-----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQL---- 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  219 qgpsGEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKL-EAQA 297
Cdd:TIGR02168  746 ----EERIA-------QLSKELTELEAEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALdELRA 810

                          170
                   ....*....|...
gi 1720412145  298 DYEEIKTELSILR 310
Cdd:TIGR02168  811 ELTLLNEEAANLR 823
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 121-301 1.66e-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: 45.84  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  121 ERQKGLQEVHIT-LAARLGEAEEKIKVLHSALKATQTELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:pfam05622  296 LGQEGSYRERLTeLQQLLEDANRRKNELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEA 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNSSIrlaccspQGPSGEKVSfalcsgpRLEAALASKDREIL-------RLLKDAQQLRHSLQ-ELE 265
Cdd:pfam05622  376 QSELQKKKEQIEELEPKQ-------DSNLAQKID-------ELQEALRKKDEDMKameerykKYVEKAKSVIKTLDpKQN 441

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1720412145  266 EVSANQIADLERQLAAKSEAIEKLQ---EKLEAQADYEE 301
Cdd:pfam05622  442 PASPPEIQALKNQLLEKDKKIEHLErdfEKSKLQREQEE 480
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
136-309 1.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  136 RLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlAC 215
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  216 CSPQGPSGEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLE- 294
Cdd:COG4372     93 QAELAQAQEELE-------SLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREEELKELEEQLEs 161

                          170
                   ....*....|....*
gi 1720412145  295 AQADYEEIKTELSIL 309
Cdd:COG4372    162 LQEELAALEQELQAL 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-297 1.91e-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: 45.53  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQKGLQEVHiTLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKA---DEVGLIMTNLEKANQR-- 189
Cdd:COG4942     43 LAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkEELAELLRALYRLGRQpp 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  190 -----------------------AEAAQREVESLREQLASVNSSIRLAccspqgpSGEKVSFAlcsgpRLEAALASKDRE 246
Cdd:COG4942    122 lalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAEL-------EAERAELE-----ALLAELEEERAA 189

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720412145  247 ILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQA 297
Cdd:COG4942    190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
131-335 1.98e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  131 ITLAARLGEAEEKIKVLHSALKATQTELLELRRKYD---EEAASKADEVGLIMTN----------LEKANQRAEAAQR-- 195
Cdd:COG3206    208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalrAQLGSGPDALPELLQSpviqqlraqlAELEAELAELSARyt 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  196 ----EVESLREQLASVNSSIRLaccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSAN- 270
Cdd:COG3206    288 pnhpDVIALRAQIAALRAQLQQ---------------------EAQRILASLEAELEALQAREASLQAQLAQLEARLAEl 346

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412145  271 -----QIADLERQLAAKSEAIEKLQEKLEaqadyeeiktELSILRAMKLAS----STCSLPQTLAKPDDPLLVA 335
Cdd:COG3206    347 peleaELRRLEREVEVARELYESLLQRLE----------EARLAEALTVGNvrviDPAVVPLKPVSPKKLLILA 410
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-207 2.26e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  116 QKNEAERQ-KGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQ 194
Cdd:COG4913    339 RLEQLEREiERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                           90
                   ....*....|...
gi 1720412145  195 REVESLREQLASV 207
Cdd:COG4913    419 RELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-298 2.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  120 AERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRR------------KYDEEAASKADEVGLIMTN---LE 184
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASsddLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  185 KANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgekvsfalcsgpRLEAALAskdrEILRLLKDAQQLRHSLQEL 264
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELE----QAEEELDELQDRLEAAEDL 742

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720412145  265 EEVSANQIADLERQLAAKSEAIEKLQEKLEAQAD 298
Cdd:COG4913    743 ARLELRALLEERFAAALGDAVERELRENLEERID 776
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-298 2.39e-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: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQKGLQ----EVHITLAA-RLGEAEEKIKVLHSALKATQTELLELRRKYDEeAASKADEVGLIMTNLEKanqR 189
Cdd:TIGR02168  207 RQAEKAERYKELKaelrELELALLVlRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEE---E 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  190 AEAAQREVESLREQLASVNSSIRLAccspqgpsGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEVSA 269
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  270 NQ-------------------------------IADLERQLAAKSEAIEKLQEKLEAQAD 298
Cdd:TIGR02168  355 SLeaeleeleaeleelesrleeleeqletlrskVAQLELQIASLNNEIERLEARLERLED 414
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 139-311 2.56e-04

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: 45.40  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  139 EAEEKIKVLHSALKATQTELLELRRKYD--------EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSs 210
Cdd:TIGR04523  278 QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES- 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  211 irlaccspqgpsgEKVSfalcsgprLEAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKSEAIEKLQ 290
Cdd:TIGR04523  357 -------------ENSE--------KQRELEEKQNEIEKLKKENQSYKQEIKNLE----SQINDLESKIQNQEKLNQQKD 411

                          170       180
                   ....*....|....*....|..
gi 1720412145  291 EKLE-AQADYEEIKTELSILRA 311
Cdd:TIGR04523  412 EQIKkLQQEKELLEKEIERLKE 433
PRK12704 PRK12704
phosphodiesterase; Provisional
 137-301 5.37e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  137 LGEAEEKIKVL-HSALKATQTELLELRRKYDEEAASKADEVglimTNLEKANQraeaaQREvESLREQLASVNssirlac 215
Cdd:PRK12704    44 LEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLL-----QKE-ENLDRKLELLE------- 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  216 cspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRhslQELEEVSANQIADLER-----QLAAKSEAIEKLQ 290
Cdd:PRK12704   107 -------------------KREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERisgltAEEAKEILLEKVE 164

                          170
                   ....*....|....*.
gi 1720412145  291 EKLEAQA-----DYEE 301
Cdd:PRK12704   165 EEARHEAavlikEIEE 180
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 115-297 5.81e-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: 44.43  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQkGLQEVHITLAARLGEAEEKIKVLHSALKAT-------QTELLELRRKYDE-----------------EAA 170
Cdd:pfam10174  298 LSKKESELL-ALQTKLETLTNQNSDCKQHIEVLKESLTAKeqraailQTEVDALRLRLEEkesflnkktkqlqdlteEKS 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  171 SKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVN---SSIRLACCSPQGPSGEKVSfALCSgprLEAALASKDREI 247
Cdd:pfam10174  377 TLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDT-ALTT---LEEALSEKERII 452

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412145  248 LRL-----------LKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLEAQA 297
Cdd:pfam10174  453 ERLkeqreredrerLEELESLKKENKDLKE----KVSALQPELTEKESSLIDLKEHASSLA 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
132-301 9.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 9.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  132 TLAARLGEAEEKIKVLHSALKATQTELLELRRKydEEAASKADEVGlimtnleKANQRAEAAQREVESLREQLASV-NSS 210
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQER--REALQRLAEYS-------WDEIDVASAEREIAELEAELERLdASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  211 IRLAccspqgpsgekvsfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKSEAIEKLQ 290
Cdd:COG4913    685 DDLA--------------------ALEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEELDELQDRLEAAE 740

                          170
                   ....*....|...
gi 1720412145  291 E--KLEAQADYEE 301
Cdd:COG4913    741 DlaRLELRALLEE 753
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-292 1.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  119 EAERQKGLQEVHITLAARLGEAEEKIKVLhSALKATQTELLELRRKYDEEAASKADEVGLIMTNLE---------KANQR 189
Cdd:COG4717    318 EEELEELLAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelraalEQAEE 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  190 AEAAQREVESLREQLASVNSSIRLAccsPQGPSGEKVSFALcsgPRLEAALASKDREILRLLKDAQQLRHSLQELEEvsA 269
Cdd:COG4717    397 YQELKEELEELEEQLEELLGELEEL---LEALDEEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEE--D 468

                          170       180
                   ....*....|....*....|...
gi 1720412145  270 NQIADLERQLAAKSEAIEKLQEK 292
Cdd:COG4717    469 GELAELLQELEELKAELRELAEE 491
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 158-305 1.99e-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: 39.99  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  158 LLELRRKYDEEAAskadevglimTNLEKANQRAEAAQREVESLREQL----ASVNSSIRlaccspQGPSGekvsfalcsg 233
Cdd:TIGR02473    7 LLDLREKEEEQAK----------LELAKAQAEFERLETQLQQLIKYReeyeQQALEKVG------AGTSA---------- 60

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412145  234 prleAALASKDREILRLLKDAQQLRHSLQELEevsaNQIADLERQLAAKS---EAIEKLQEKLEAQADYEEIKTE 305
Cdd:TIGR02473   61 ----LELSNYQRFIRQLDQRIQQQQQELALLQ----QEVEAKRERLLEARrelKALEKLKEKKQKEYRAEEAKRE 127
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-311 2.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  133 LAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEaaSKADEVGLIMTNLEKAN-QRAEAAQREVESLREQLASVNSSI 211
Cdd:PRK03918   464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEI 541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  212 R-LACCSPQGPSGEKVSFALCSGPR-LEAALASKDREILRL-LKDAQQLRHSLQELEEV--SANQIADLERQLAAKSEAI 286
Cdd:PRK03918   542 KsLKKELEKLEELKKKLAELEKKLDeLEEELAELLKELEELgFESVEELEERLKELEPFynEYLELKDAEKELEREEKEL 621

                          170       180
                   ....*....|....*....|....*.
gi 1720412145  287 EKLQEKL-EAQADYEEIKTELSILRA 311
Cdd:PRK03918   622 KKLEEELdKAFEELAETEKRLEELRK 647
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-310 2.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  117 KNEAERqkgLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRK---YDEEAASKADEVGLIMTNLEKANQRAEAA 193
Cdd:PRK02224   341 NEEAES---LREDADDLEERAEELREEAAELESELEEAREAVEDRREEieeLEEEIEELRERFGDAPVDLGNAEDFLEEL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  194 QREVESLREQLASVNSSIRlaccspqgpsgeKVSFALCSGPRLEAAlaSKDREILRLLKDAQQLrHSLQELEEvsanQIA 273
Cdd:PRK02224   418 REERDELREREAELEATLR------------TARERVEEAEALLEA--GKCPECGQPVEGSPHV-ETIEEDRE----RVE 478

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720412145  274 DLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILR 310
Cdd:PRK02224   479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE 515
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
149-311 2.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  149 SALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLAsvnssirlaccspqgpsgekvsf 228
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE----------------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  229 alcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEvsanQIADLERQLAAKSEAIEKLQEKLEA-QADYEEIKTELS 307
Cdd:COG4372     63 ------QLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQEELEElQKERQDLEQQRK 132


                   ....
gi 1720412145  308 ILRA 311
Cdd:COG4372    133 QLEA 136
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 178-336 3.05e-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: 41.67  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  178 LIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpsgekvsfalcsgprleAALASKDREILRLLKDAQQL 257
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKEL--------------------------AALKKEEKALLKQLAALERR 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  258 RHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQadyeeiKTELS-ILRAMKLASSTcSLPQTLAKPDDPLLVAK 336
Cdd:COG4942     64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ------KEELAeLLRALYRLGRQ-PPLALLLSPEDFLDAVR 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-289 3.11e-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: 42.35  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  120 AERQKGLQEVHITLAARLGEAEEKIKVLHSALKatqtELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVES 199
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  200 LREQLASVNSSI-----RLACCSPQGPSGEKVSF--ALCSGPRLEAALASKDREILRLLKDAQQL----RHSLQELEEVS 268
Cdd:TIGR02168  920 LREKLAQLELRLeglevRIDNLQERLSEEYSLTLeeAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELK 999

                          170       180
                   ....*....|....*....|....*..
gi 1720412145  269 ------ANQIADLERQLAAKSEAIEKL 289
Cdd:TIGR02168 1000 erydflTAQKEDLTEAKETLEEAIEEI 1026
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 139-371 3.64e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.13  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  139 EAEEKIKVLHSALKATQtellelrrkydEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLasvnssIRLaccsp 218
Cdd:pfam12128  601 ELRERLDKAEEALQSAR-----------EKQAAAEEQLVQANGELEKASREETFARTALKNARLDL------RRL----- 658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  219 qgpSGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQ---------------IADLERQLAAKS 283
Cdd:pfam12128  659 ---FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkreartekqaywqvvEGALDAQLALLK 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  284 EAIEKLQEKLEAQADY--EEIKTELSIL-----RAMKLASSTCSLPQTL--AKPDDPLLVAKDVFFPTQkFLLEKPALLA 354
Cdd:pfam12128  736 AAIAARRSGAKAELKAleTWYKRDLASLgvdpdVIAKLKREIRTLERKIerIAVRRQEVLRYFDWYQET-WLQRRPRLAT 814

                          250
                   ....*....|....*..
gi 1720412145  355 SPEEDPSEDDSIKGSLG 371
Cdd:pfam12128  815 QLSNIERAISELQQQLA 831
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
134-305 3.65e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  134 AARLGEAEEKIKVLHSALKATQTELLELRRKYD--EEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNssi 211
Cdd:PRK02224   467 VETIEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR--- 543

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  212 rlaccspqgpsgEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEV--SANQIADLERQLAAKSEAIEKL 289
Cdd:PRK02224   544 ------------ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADAEDEIERL 611

                          170
                   ....*....|....*.
gi 1720412145  290 QEKLEAQADYEEIKTE 305
Cdd:PRK02224   612 REKREALAELNDERRE 627
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 235-311 3.85e-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: 3.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412145  235 RLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQeklEAQADYEEIKTELSILRA 311
Cdd:pfam07926    5 SLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQ---ALREELNELKAEIAELKA 78
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
133-311 3.92e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.58  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  133 LAARLGEAEEKIKVLHSALKATQTELLELRRkydeeaaskadEVGLIMTNLEKANQRAEAAQREVESLREQLasvnssir 212
Cdd:COG1842     14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQ-----------ALAQVIANQKRLERQLEELEAEAEKWEEKA-------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  213 laccspqgpsgekvsfalcsgprlEAALaSKDREilRLLKDAQQLRHSLQeleevsaNQIADLERQLAAKSEAIEKLQEK 292
Cdd:COG1842     75 ------------------------RLAL-EKGRE--DLAREALERKAELE-------AQAEALEAQLAQLEEQVEKLKEA 120

                          170       180
                   ....*....|....*....|
gi 1720412145  293 L-EAQADYEEIKTELSILRA 311
Cdd:COG1842    121 LrQLESKLEELKAKKDTLKA 140
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 244-311 4.53e-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: 4.53e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412145  244 DREILRLLKDAQQLRHSLQELEEVSAN---QIADLERQLAAKSEAIEKLQEKLE-AQADYEEIKTELSILRA 311
Cdd:COG1579      2 MPEDLRALLDLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELEdLEKEIKRLELEIEEVEA 73
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
1113-1171 4.85e-03

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 39.34  E-value: 4.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412145 1113 AKKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRRE 1171
Cdd:COG5576     51 PKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 106-306 5.43e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  106 EDTLvtdTLLQKNEAERQKglqevhitLAARLGEAEEKIkvlhsaLKATQTELLELRRKYDEEAASKADEVGLIMTNLEK 185
Cdd:TIGR00606  268 DNEI---KALKSRKKQMEK--------DNSELELKMEKV------FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEK 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  186 ANQ-RAEAAQREVESLREQlasvnSSIRLACCSPQGPSGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQEL 264
Cdd:TIGR00606  331 LNKeRRLLNQEKTELLVEQ-----GRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQED 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720412145  265 EEVSANQ-IADLERQLAAKSEAIEKLQEKLEAQADYEEIKTEL 306
Cdd:TIGR00606  406 EAKTAAQlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-344 5.76e-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: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  115 LQKNEAERQKGLQEvhitLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAAskadEVGLIMTNLEKANQRAEAAQ 194
Cdd:TIGR02169  845 LKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLRELERKIEELEAQIEKKR 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  195 REVESLREQLASVNSsiRLACCSPQGPSGEKVSFALCSGPRLEAALASKDREIlrllkdaqqlrhslQELEEVSANQIAD 274
Cdd:TIGR02169  917 KRLSELKAKLEALEE--ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI--------------RALEPVNMLAIQE 980

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  275 LERQLAAKSEAIEKlQEKLEAQ--------ADYEEIKTEL------SILRAMK-----LASSTCSLpqTLAKPDDPL--- 332
Cdd:TIGR02169  981 YEEVLKRLDELKEK-RAKLEEErkaileriEEYEKKKREVfmeafeAINENFNeifaeLSGGTGEL--ILENPDDPFagg 1057

                          250
                   ....*....|....
gi 1720412145  333 --LVAKDVFFPTQK 344
Cdd:TIGR02169 1058 leLSAKPKGKPVQR 1071
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 235-296 5.94e-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: 39.42  E-value: 5.94e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412145  235 RLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQ 296
Cdd:pfam06785  101 RLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQ 162
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
118-313 6.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  118 NEAERQKGLQEvhitlaARLGEAEEKIKVLHSALKATQTELLELRRKYDE--EAASKADEVGLIMTNLEKANQRAEAAQR 195
Cdd:PRK03918   241 EELEKELESLE------GSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEK 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412145  196 EVESLREQLASVNSSIrlaccspqgpsgEKVSfalcsgpRLEAALASKDREILRLLKDAQQLRHSLQELEEVSA--NQIA 273
Cdd:PRK03918   315 RLSRLEEEINGIEERI------------KELE-------EKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkEELE 375

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720412145  274 DLERQLAAKSeaIEKLQEKLE-AQADYEEIKTELSILRAMK 313
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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