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Conserved domains on  [gi|1622947863|ref|XP_028705674|]
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TNFAIP3-interacting protein 1 isoform X6 [Macaca mulatta]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
246-477 9.83e-12

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 9.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  246 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 322
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  323 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 402
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863  403 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 477
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
DUF3584 super family cl37832
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
110-369 6.74e-06

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.


The actual alignment was detected with superfamily member pfam12128:

Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 49.45  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  110 QRLETTLSVCAEEPDHSQLFTHLGRMALEFNRL----------ASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLDK 176
Cdd:pfam12128  621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrrlfdekqSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQA 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  177 GLEQRDQAAERLREENLELKKLLMSNgnkegASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQ 256
Cdd:pfam12128  701 WLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  257 QRSEL------LEVNKQ-------WDQH-FRSMKQQYEQKITELRQKLADLQKQVTDLEAERE------QKQRDFDRKLL 316
Cdd:pfam12128  776 EIRTLerkierIAVRRQevlryfdWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKlrraklEMERKASEKQQ 855
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863  317 ------LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam12128  856 vrlsenLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
246-477 9.83e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 9.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  246 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 322
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  323 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 402
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863  403 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 477
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
281-479 8.96e-11

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: 64.01  E-value: 8.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 281 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 360
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 361 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 437
Cdd:COG4942    96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622947863 438 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREANRQQKRKAKAS 479
Cdd:COG4942   176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
400-448 2.18e-08

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 51.58  E-value: 2.18e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622947863 400 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 448
Cdd:cd09803    34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-446 4.21e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 177 GLEQRDQAAERL-------REENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVTAGKVPEVAA-LGAAE 248
Cdd:PRK03918  156 GLDDYENAYKNLgevikeiKRRIERLEKFIKRTENIEE--------LIKEKEKELEEVLREINEISSELPELREeLEKLE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 249 KKVKMLEQQRSELLEVNKQWDQHFRSMK------QQYEQKITELRQKLADLQKQVTDLE-----AEREQKQRDFDRKLLL 317
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLD 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 318 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQTPPSSPPTAFGSpega 394
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTG---- 383
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622947863 395 galLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 446
Cdd:PRK03918  384 ---LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
408-450 2.04e-06

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 46.52  E-value: 2.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622947863 408 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 450
Cdd:pfam16516  55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
110-369 6.74e-06

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: 49.45  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  110 QRLETTLSVCAEEPDHSQLFTHLGRMALEFNRL----------ASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLDK 176
Cdd:pfam12128  621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrrlfdekqSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQA 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  177 GLEQRDQAAERLREENLELKKLLMSNgnkegASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQ 256
Cdd:pfam12128  701 WLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  257 QRSEL------LEVNKQ-------WDQH-FRSMKQQYEQKITELRQKLADLQKQVTDLEAERE------QKQRDFDRKLL 316
Cdd:pfam12128  776 EIRTLerkierIAVRRQevlryfdWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKlrraklEMERKASEKQQ 855
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863  317 ------LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam12128  856 vrlsenLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
263-373 1.87e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.80  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 341
Cdd:smart00935  18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622947863  342 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 373
Cdd:smart00935  77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
162-199 2.00e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 43.43  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622947863 162 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 199
Cdd:PRK13922   73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
246-477 9.83e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 9.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  246 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 322
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  323 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 402
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863  403 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 477
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
281-479 8.96e-11

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: 64.01  E-value: 8.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 281 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 360
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 361 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 437
Cdd:COG4942    96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622947863 438 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREANRQQKRKAKAS 479
Cdd:COG4942   176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
283-478 1.45e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 283 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 362
Cdd:COG1196   195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 363 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 442
Cdd:COG1196   275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622947863 443 EKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
277-448 2.04e-10

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: 61.09  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 357 REYQ--EKEI---QRLNKALEEALsiqtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErm 431
Cdd:COG1579    89 KEYEalQKEIeslKRRISDLEDEI------------------LELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
                         170
                  ....*....|....*..
gi 1622947863 432 nEEKEELKKQVEKLQAQ 448
Cdd:COG1579   149 -EELAELEAELEELEAE 164
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
248-467 4.25e-10

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: 62.73  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 317
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 318 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 396
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947863 397 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 467
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
138-446 6.24e-10

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: 62.38  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGQPGSPKM 217
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  218 EGAGKKAVAGQQQASVTAGK---VPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYE---QKITELRQKLA 291
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdleEQIEELSEDIE 855
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  292 DLQKQVTDLEAEREQKQRDFDRKL-LLAKSKIEME--ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE-YQEK----- 362
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLnERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAqLELRlegle 935
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  363 -EIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAgallrKQELvtqnELLKQQVKIF-------EEDFQRERSDRERMN 432
Cdd:TIGR02168  936 vRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEA-----RRRL----KRLENKIKELgpvnlaaIEEYEELKERYDFLT 1006
                          330
                   ....*....|....
gi 1622947863  433 EEKEELKKQVEKLQ 446
Cdd:TIGR02168 1007 AQKEDLTEAKETLE 1020
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
117-482 8.78e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.93  E-value: 8.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  117 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLEL 195
Cdd:TIGR02169  667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  196 KKLLMSNGNKegasgqpgspKMEGAGKKAVAGQQQASVTAGKVpEVAALGA--AEKKVKMLEQQRSELLEVNKQWDQHFR 273
Cdd:TIGR02169  747 SSLEQEIENV----------KSELKELEARIEELEEDLHKLEE-ALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  274 SMkqqyEQKITELRQKLADLQKQVTDLEAEREQKQrdfDRKLLLAKsKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPL 353
Cdd:TIGR02169  816 EI----EQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  354 TRQREYQEKEIQRLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 432
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622947863  433 EEkEELKKQVEKLQAQV-TLSNAQLKAFKD-EEKAREANRQQKRKAKASGER 482
Cdd:TIGR02169  952 SL-EDVQAELQRVEEEIrALEPVNMLAIQEyEEVLKRLDELKEKRAKLEEER 1002
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-476 1.11e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  283 ITELRQKLADLQKQVT------DLEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQD 348
Cdd:TIGR02168  195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  349 QLSPLtrqreyqEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 428
Cdd:TIGR02168  275 EVSEL-------EEEIEELQKELYALANEI---------------SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622947863  429 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-376 1.52e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgqpgspkm 217
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 218 egAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 294
Cdd:COG1196   329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 295 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 371
Cdd:COG1196   407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                  ....*
gi 1622947863 372 EEALS 376
Cdd:COG1196   487 AEAAA 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-462 1.84e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  275 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 351
Cdd:COG4913    247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  352 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 409
Cdd:COG4913    327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622947863  410 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:COG4913    396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
242-448 1.85e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.70  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR----- 313
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllral 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 314 ---------KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppssp 384
Cdd:COG4942   114 yrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE-------- 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947863 385 ptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 448
Cdd:COG4942   186 --------------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
272-478 1.85e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 272 FRSMKQQYEQKITELR-QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQL 350
Cdd:COG1196   215 YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEE----LEAELAELEAELEELRLELEELELELEEAQAEE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 351 SPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRER 430
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEE----------------------RLEELEEELAELEEELEELEEELEELEEELEE 348
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622947863 431 MNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
400-448 2.18e-08

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 51.58  E-value: 2.18e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622947863 400 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 448
Cdd:cd09803    34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-446 4.21e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 177 GLEQRDQAAERL-------REENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVTAGKVPEVAA-LGAAE 248
Cdd:PRK03918  156 GLDDYENAYKNLgevikeiKRRIERLEKFIKRTENIEE--------LIKEKEKELEEVLREINEISSELPELREeLEKLE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 249 KKVKMLEQQRSELLEVNKQWDQHFRSMK------QQYEQKITELRQKLADLQKQVTDLE-----AEREQKQRDFDRKLLL 317
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLD 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 318 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQTPPSSPPTAFGSpega 394
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTG---- 383
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622947863 395 galLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 446
Cdd:PRK03918  384 ---LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-481 5.68e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 5.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  357 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKE 436
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622947863  437 ELKkqVEKLQAQVTLSNAQlkaFKDEEKAREANRQQKRKAKASGE 481
Cdd:TIGR02168  814 LLN--EEAANLRERLESLE---RRIAATERRLEDLEEQIEELSED 853
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
276-478 6.07e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 6.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 276 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 355
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 356 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 434
Cdd:COG3883    92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622947863 435 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
PTZ00121 PTZ00121
MAEBL; Provisional
138-478 6.45e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 6.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKLLMSNGNKEGASGQPGSPKM 217
Cdd:PTZ00121  1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKA 1317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  218 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQV 297
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE----KKKEEAKKKADAAKKKAEEKKKA 1393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  298 TDLE--AEREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKylQDQLSPLTRQREYQEKEIQRLNKALEEAL 375
Cdd:PTZ00121  1394 DEAKkkAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  376 SIQTPPSSPPTAFGSPEG---AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQV 449
Cdd:PTZ00121  1471 KADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADE 1550
                          330       340
                   ....*....|....*....|....*....
gi 1622947863  450 TLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
280-478 1.70e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  280 EQKITELRQKLADLQKQVTDLEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVKYLQDQLSPLTRQREY 359
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  360 QEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 432
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1622947863  433 EEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
155-477 3.68e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 155 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVT 234
Cdd:COG4717    43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 235 AGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 314
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 315 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 383
Cdd:COG4717   187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 384 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQL-KAFKDE 462
Cdd:COG4717   267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlELLDRI 346
                         330
                  ....*....|....*
gi 1622947863 463 EKAREANRQQKRKAK 477
Cdd:COG4717   347 EELQELLREAEELEE 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
132-442 4.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 4.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkEGASGQ 211
Cdd:TIGR02169  718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL-------EARLSH 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  212 PGSPKMEGAGKKAvagQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 287
Cdd:TIGR02169  791 SRIPEIQAELSKL---EEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  288 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 367
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  368 NKALEEalsiqTPPSSPP---------------TAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEdfqreRSDRERMN 432
Cdd:TIGR02169  940 KGEDEE-----IPEEELSledvqaelqrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE-----RKAILERI 1009
                          330
                   ....*....|
gi 1622947863  433 EEKEELKKQV 442
Cdd:TIGR02169 1010 EEYEKKKREV 1019
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
276-442 8.90e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.14  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 276 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 353
Cdd:PRK00409  529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 354 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 421
Cdd:PRK00409  602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
                         170       180
                  ....*....|....*....|.
gi 1622947863 422 qrerSDRERMNEEKEELKKQV 442
Cdd:PRK00409  677 ----SDLEKIQKPKKKKKKKP 693
PTZ00121 PTZ00121
MAEBL; Provisional
134-492 1.23e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  134 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQP 212
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  213 GSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 287
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  288 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 364
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  365 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNEllkqQVKIFEEDfqrERSDRERMNEEKEELKKQVEK 444
Cdd:PTZ00121  1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAE----ELKKKEAE---EKKKAEELKKAEEENKIKAEE 1734
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1622947863  445 LQAqvtlsnaqlKAFKDEEKAREANRQQKRKAKASGERYHVEPHPEHL 492
Cdd:PTZ00121  1735 AKK---------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
PTZ00121 PTZ00121
MAEBL; Provisional
143-477 1.63e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  143 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGA 220
Cdd:PTZ00121  1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  221 GKKAVAGQQQASVTAGKVPEvaALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQ--------- 288
Cdd:PTZ00121  1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKaaeakkkad 1513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  289 --KLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 366
Cdd:PTZ00121  1514 eaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  367 LNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNEllkQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQ 446
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKK 1669
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1622947863  447 AQVTLSNAQlKAFKDEEKAREANRQQKRKAK 477
Cdd:PTZ00121  1670 AEEDKKKAE-EAKKAEEDEKKAAEALKKEAE 1699
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-445 2.04e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  244 LGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 320
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  321 KIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGAGALL 398
Cdd:COG4913    739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYL 818
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622947863  399 RKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 445
Cdd:COG4913    819 ALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
408-450 2.04e-06

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 46.52  E-value: 2.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622947863 408 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 450
Cdd:pfam16516  55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
138-378 2.38e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENlelKKLLMSNGNKEGasgqpgspkM 217
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELES---------L 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  218 EGAGKKAVAGQQQASvtagkvpevAALGAAEKKvkmLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 297
Cdd:TIGR02168  357 EAELEELEAELEELE---------SRLEELEEQ---LETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  298 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 376
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496

                   ..
gi 1622947863  377 IQ 378
Cdd:TIGR02168  497 LQ 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
150-477 2.75e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  150 EQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQaaeRLREENLELKKLLmsnGNKEGASGQpgspKMEGAGKKAVAGQQ 229
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERLRREREKAERYQAL---LKEKREYEGYELL---KEKEALERQ----KEAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  230 QASVTAgkvpevaalgAAEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AEREQ 306
Cdd:TIGR02169  253 LEKLTE----------EISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  307 KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppssppt 386
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------- 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  387 afgspegagallrkqelvTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:TIGR02169  383 ------------------TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
                          330
                   ....*....|....*.
gi 1622947863  463 -EKAREANRQQKRKAK 477
Cdd:TIGR02169  443 kEDKALEIKKQEWKLE 458
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
248-472 2.82e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 327
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 328 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 407
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863 408 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 472
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
132-448 3.25e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 211
Cdd:pfam02463  675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  212 PGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 291
Cdd:pfam02463  755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  292 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 361
Cdd:pfam02463  835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  362 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 425
Cdd:pfam02463  915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
                          330       340
                   ....*....|....*....|...
gi 1622947863  426 SDRERMNEEKEELKKQVEKLQAQ 448
Cdd:pfam02463  995 LEKERLEEEKKKLIRAIIEETCQ 1017
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
248-481 4.70e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 327
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 328 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 403
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 404 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREANRQQ 472
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQI 581

                  ....*....
gi 1622947863 473 KRKAKASGE 481
Cdd:pfam17380 582 VESEKARAE 590
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
141-477 4.85e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 4.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  141 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEga 220
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-- 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  221 gkkavagqqqasvtagkvpEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 300
Cdd:pfam02463  252 -------------------EIESSKQEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  301 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 380
Cdd:pfam02463  310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  381 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 460
Cdd:pfam02463  386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
                          330
                   ....*....|....*..
gi 1622947863  461 DEEKAREANRQQKRKAK 477
Cdd:pfam02463  465 LELKKSEDLLKETQLVK 481
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
138-397 5.56e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgqpgspKM 217
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 218 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 297
Cdd:COG4942    99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 298 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 377
Cdd:COG4942   167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
                         250       260
                  ....*....|....*....|
gi 1622947863 378 QTPPSSPPTAFGSPEGAGAL 397
Cdd:COG4942   236 AAAAAERTPAAGFAALKGKL 255
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
110-369 6.74e-06

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: 49.45  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  110 QRLETTLSVCAEEPDHSQLFTHLGRMALEFNRL----------ASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLDK 176
Cdd:pfam12128  621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrrlfdekqSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQA 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  177 GLEQRDQAAERLREENLELKKLLMSNgnkegASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQ 256
Cdd:pfam12128  701 WLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  257 QRSEL------LEVNKQ-------WDQH-FRSMKQQYEQKITELRQKLADLQKQVTDLEAERE------QKQRDFDRKLL 316
Cdd:pfam12128  776 EIRTLerkierIAVRRQevlryfdWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKlrraklEMERKASEKQQ 855
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863  317 ------LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam12128  856 vrlsenLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
263-492 9.35e-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: 48.90  E-value: 9.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  263 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 340
Cdd:TIGR02168  197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  341 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 417
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863  418 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdEEKAREANRQQKRKAKASGERYHVEPHPEHL 492
Cdd:TIGR02168  347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQL--ETLRSKVAQLELQIASLNNEIERLEARLERL 412
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
248-455 9.39e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 9.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQKQVTDLEAE---------------REQKQR 309
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 310 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQTP 380
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS---DLEDE 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 381 PSSPPTAFGSPEGAGALLRKQELV-----TQNELLKQQVKiFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQ 455
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIeelkqTQKSLKKKQEE-KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-377 1.47e-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: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  141 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLReenlELKKLLMSNGnkegasgqpgspkmega 220
Cdd:COG4913    278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNG----------------- 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  221 gkkavaGQQqasvtagkvpevaaLGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL 300
Cdd:COG4913    337 ------GDR--------------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947863  301 EAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRqreyqekEIQRLNKALEEALSI 377
Cdd:COG4913    397 EEELEALEEALAEA-----------EAALRDLRRELRELEAEIASLERRKSNIPA-------RLLALRDALAEALGL 455
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
269-472 1.48e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 269 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 343
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 344 KYLQDQL-------SPLTRQREYQE--KEIQRLNKALEEALSIQTPpsspptafGSPEGAGAllrKQELVTQNELLKQQV 414
Cdd:COG3206   243 AALRAQLgsgpdalPELLQSPVIQQlrAQLAELEAELAELSARYTP--------NHPDVIAL---RAQIAALRAQLQQEA 311
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947863 415 KifeEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 472
Cdd:COG3206   312 Q---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
120-448 1.84e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 120 AEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkll 199
Cdd:pfam17380 327 AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE-------- 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 200 msngnkegasgqpgspkMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSEllEVNKQWDQHFRSMKQQY 279
Cdd:pfam17380 398 -----------------LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREMERVRLEEQER 458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 280 EQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREY 359
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKL 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 360 QEKEIQRLNKALEEALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELK 439
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMR 579

                  ....*....
gi 1622947863 440 KQVEKLQAQ 448
Cdd:pfam17380 580 QIVESEKAR 588
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
138-457 2.02e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  138 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGA------ 208
Cdd:pfam15921  518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAmqveka 593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  209 --SGQPGSPKME-------GAGKKAVAGQQQASVTAGKVPEVAALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 276
Cdd:pfam15921  594 qlEKEINDRRLElqefkilKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 343
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  344 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 423
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1622947863  424 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 457
Cdd:pfam15921  821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
248-475 2.52e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELlevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK------ 321
Cdd:TIGR04523 186 QKNIDKIKNKLLKL--------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnq 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 322 -IEMEETDKEQLTAEAKELRQ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegag 395
Cdd:TIGR04523 258 lKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ----------------- 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 396 allRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 466
Cdd:TIGR04523 320 ---EKKLEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396

                  ....*....
gi 1622947863 467 EANRQQKRK 475
Cdd:TIGR04523 397 ESKIQNQEK 405
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-374 2.52e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 149 NEQRTSILQTLcEQLRKENEALKAKLdkglEQRDQAAERLREENlelkKLLMSNGNKEGASGQpgspkmegagkKAVAGQ 228
Cdd:COG3206   167 ELRREEARKAL-EFLEEQLPELRKEL----EEAEAALEEFRQKN----GLVDLSEEAKLLLQQ-----------LSELES 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 229 QQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVT 298
Cdd:COG3206   227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIA 301
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863 299 DLEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 374
Cdd:COG3206   302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
71-464 3.21e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.04  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863   71 EFEVVTPEEQSSPPENSSHANETVLGPLPHEDGNLMLHLQRLETTLSVCAEEPDhsqlfthlGRMALEFNRLASKVHKNE 150
Cdd:pfam15921  390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLE 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  151 QRTSI---LQTLCEQLRKENEALKAK-------------LDKGLEQRDQAAERLREE--------NLELKKL--LMSNGN 204
Cdd:pfam15921  462 KVSSLtaqLESTKEMLRKVVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEitklrsrvDLKLQELqhLKNEGD 541
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  205 K-EGASGQPGSPKMEGAGKKAVAG---QQQASVT--AGKVPEVAALGAAEKKV--KMLEQQRSELlevnkqwdQHFRSMK 276
Cdd:pfam15921  542 HlRNVQTECEALKLQMAEKDKVIEilrQQIENMTqlVGQHGRTAGAMQVEKAQleKEINDRRLEL--------QEFKILK 613
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:pfam15921  614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRN 682
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  357 REYQEKEIQRLNKALEEAL-SIQTPPSSPPTAFGSPEGAGALLRK-----QELVT----QNELLKQQVKIFEEDFQRERS 426
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITakrgQIDALQSKIQFLEEAMTNANK 762
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1622947863  427 DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEK 464
Cdd:pfam15921  763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
243-347 3.41e-05

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 46.13  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 243 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 315
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622947863 316 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 347
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
140-444 3.93e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 140 NRLASKVHKNEQRTSILQTLCEQLRKENEALkakldkgleqrDQAAERLREENLELKKLLMSNGNKEGASgqpgSPKMEG 219
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELL-----------EKEIERLKETIIKNNSEIKDLTNQDSVK----ELIIKN 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 220 AGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTD 299
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEK 528
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 300 LEAE---REQKQRDFDRKLL-----LAKSKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 360
Cdd:TIGR04523 529 LESEkkeKESKISDLEDELNkddfeLKKENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 361 EKEIQRLNKALEEAlsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 440
Cdd:TIGR04523 609 EKKISSLEKELEKA---------------KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673

                  ....
gi 1622947863 441 QVEK 444
Cdd:TIGR04523 674 KIDD 677
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
280-476 4.16e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  280 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 351
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  352 PLTRQREYQEKEIQRLNKALEealsiqtppsspptafgspegagallrkqELVTQNELLKQQVKIFEEDFQRERSDRERM 431
Cdd:COG4913    689 ALEEQLEELEAELEELEEELD-----------------------------ELKGEIGRLEKELEQAEEELDELQDRLEAA 739
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1622947863  432 NE-EKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:COG4913    740 EDlARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
109-492 4.71e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 4.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  109 LQRLETTLsVCAEEPDHSQLFTHLGRMALEFNRLASKVHKneqrtsilqtLCEQLRKENEALKAKLdkgLEQRDQAAERL 188
Cdd:pfam15921  186 LQEIRSIL-VDFEEASGKKIYEHDSMSTMHFRSLGSAISK----------ILRELDTEISYLKGRI---FPVEDQLEALK 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  189 REENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQW 268
Cdd:pfam15921  252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLESTVSQL 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  269 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR------DFDRKLLLAKSKIEME-ETDKEQltaeAKELRQ 341
Cdd:pfam15921  330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLEKEQ----NKRLWD 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  342 KVKYLQDQLSPLTRQREYQEKEIQRLNkaleealsiqtppsspptafgspegagALLRKQELVTQNELLKQQVKI--FEE 419
Cdd:pfam15921  406 RDTGNSITIDHLRRELDDRNMEVQRLE---------------------------ALLKAMKSECQGQMERQMAAIqgKNE 458
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  420 DFQRERSDRERMNEEKEELKKQVEKLQA-QVTLSNAQ------LKAFKDEEKAREANRQQKRKAKAS-----GERYHVEP 487
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKN 538

                   ....*
gi 1622947863  488 HPEHL 492
Cdd:pfam15921  539 EGDHL 543
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-482 4.97e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  287 RQKLADLQKQVTDLEAEREQkqrdfdrklllakskiemeetdkeqLTAEAKELRQKVKYLQDQLSPLTRQREYQ------ 360
Cdd:COG4913    609 RAKLAALEAELAELEEELAE-------------------------AEERLEALEAELDALQERREALQRLAEYSwdeidv 663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  361 ---EKEIQRLNKALEEALSiqtppsspptafGSPEgagalLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEE 437
Cdd:COG4913    664 asaEREIAELEAELERLDA------------SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGR 717
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622947863  438 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 482
Cdd:COG4913    718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
PRK12704 PRK12704
phosphodiesterase; Provisional
237-367 5.64e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 237 KVPEVAALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 308
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863 309 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 367
Cdd:PRK12704   96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
145-447 6.62e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 145 KVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmSNGNKEGASGQPGSPKMEgagkka 224
Cdd:PRK03918  487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLA------ 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 225 vagqqqasvtagkvpevaalgAAEKKVKMLEQQRSELLevNKQWDQHFRSMKQqYEQKITELR---QKLADLQKQVTDLE 301
Cdd:PRK03918  560 ---------------------ELEKKLDELEEELAELL--KELEELGFESVEE-LEERLKELEpfyNEYLELKDAEKELE 615
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 302 AEREqkqrdfdrKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQdqlspltrqREYQEKEIQRLNKALEEAlsiqtpp 381
Cdd:PRK03918  616 REEK--------ELKKLEEELDKAFEELAETEKRLEELRKELEELE---------KKYSEEEYEELREEYLEL------- 671
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947863 382 sspptafgSPEGAGALLRKQELvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQA 447
Cdd:PRK03918  672 --------SRELAGLRAELEEL----EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
230-332 6.63e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.10  E-value: 6.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  230 QASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 309
Cdd:PRK11448   140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
                           90       100
                   ....*....|....*....|...
gi 1622947863  310 DFDRKlllAKSKIEMEETDKEQL 332
Cdd:PRK11448   220 EITDQ---AAKRLELSEEETRIL 239
mukB PRK04863
chromosome partition protein MukB;
258-461 6.67e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  258 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 337
Cdd:PRK04863   491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  338 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 412
Cdd:PRK04863   562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622947863  413 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 461
Cdd:PRK04863   635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-373 9.90e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 9.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 211
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 212 PGSPKMEGAGKKAVAGQQQASVtAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLA 291
Cdd:PRK03918  247 LESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 292 DLQKQVTDLEA------EREQKQRDFDRKL--------LLAKSKIEMEETDK----------EQLTAEAKELRQKVKYLQ 347
Cdd:PRK03918  325 GIEERIKELEEkeerleELKKKLKELEKRLeeleerheLYEEAKAKKEELERlkkrltgltpEKLEKELEELEKAKEEIE 404
                         250       260
                  ....*....|....*....|....*.
gi 1622947863 348 DQLSPLTRQREYQEKEIQRLNKALEE 373
Cdd:PRK03918  405 EEISKITARIGELKKEIKELKKAIEE 430
PTZ00121 PTZ00121
MAEBL; Provisional
134-435 1.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  134 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERlreENLELKKLLMSNGNKEGASGQPG 213
Cdd:PTZ00121  1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVM 1598
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  214 SPKMEGAGKKAvagqQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADL 293
Cdd:PTZ00121  1599 KLYEEEKKMKA----EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  294 QKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 371
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947863  372 EEALSIQTppsspptafgspegagalLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 435
Cdd:PTZ00121  1754 EEKKKIAH------------------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
144-396 1.12e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 144 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGQPGSPKMEGAGKK 223
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 224 AVAGQQQASVTAGKVPEV-------AALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 296
Cdd:COG3883    91 RARALYRSGGSVSYLDVLlgsesfsDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 297 VTDLEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 376
Cdd:COG3883   163 KAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
                         250       260
                  ....*....|....*....|
gi 1622947863 377 IQTPPSSPPTAFGSPEGAGA 396
Cdd:COG3883   225 AAAAAAAAAAAAAAAAAAAA 244
46 PHA02562
endonuclease subunit; Provisional
244-484 1.40e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.01  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 244 LGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSKIE 323
Cdd:PHA02562  190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIK 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 324 MEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppssppta 387
Cdd:PHA02562  269 SK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK-------- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 388 fgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARe 467
Cdd:PHA02562  338 -----------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI- 391
                         250
                  ....*....|....*..
gi 1622947863 468 anrqQKRKAKASGERYH 484
Cdd:PHA02562  392 ----VKTKSELVKEKYH 404
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
263-373 1.87e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.80  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 341
Cdd:smart00935  18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622947863  342 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 373
Cdd:smart00935  77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
162-199 2.00e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 43.43  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622947863 162 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 199
Cdd:PRK13922   73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
162-343 2.10e-04

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: 43.37  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 162 QLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQpgspkmeGAGKKAVAGQQQASVTAGKvpEV 241
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-------VEARIKKYEEQLGNVRNNK--EY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALgaaEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK 321
Cdd:COG1579    92 EAL---QKEIESLKRRISDL------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
                         170       180
                  ....*....|....*....|..
gi 1622947863 322 IEMEETDKEQLTAEAKELRQKV 343
Cdd:COG1579   151 LAELEAELEELEAEREELAAKI 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
122-396 2.31e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 122 EPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMS 201
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 202 NgNKEGASGQPGSpkmegagkkAVAGQQQASVTAGKVPEVAALGAAEKkvKMLEQQRSELLEVNKQwdqhfrsmKQQYEQ 281
Cdd:COG3883    95 L-YRSGGSVSYLD---------VLLGSESFSDFLDRLSALSKIADADA--DLLEELKADKAELEAK--------KAELEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 282 KITELRQKLADLQKQVTDLEAEREQKQrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQE 361
Cdd:COG3883   155 KLAELEALKAELEAAKAELEAQQAEQE----ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622947863 362 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGA 396
Cdd:COG3883   231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
242-474 2.61e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLA 318
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREE--------LEQLEEELEQARSELEQLEEELEELNEQLQAAQaelAQAQEELESL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 319 KSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALSIQTPPSSPPTAFGSPEGA 394
Cdd:COG4372   107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqEELAALEQELQALSEAEAEQALD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 395 GALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKR 474
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
PRK11281 PRK11281
mechanosensitive channel MscK;
161-433 2.86e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  161 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgqpgspkmegagkkAVAGQQQASVTAgkvpE 240
Cdd:PRK11281    52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  241 VAALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 307
Cdd:PRK11281   103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  308 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 372
Cdd:PRK11281   168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947863  373 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 433
Cdd:PRK11281   248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
Filament pfam00038
Intermediate filament protein;
250-482 2.86e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 250 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 325
Cdd:pfam00038  19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 326 ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAgallRKQELVT 405
Cdd:pfam00038  95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAA----RKLDLTS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 406 QNELLKQQvkiFEEDFQRERSDRErmneekEELKKQVEKLQAQVTLSNAQLKAFKDEEK-------AREANRQQKRKAKA 478
Cdd:pfam00038 171 ALAEIRAQ---YEEIAAKNREEAE------EWYQSKLEELQQAAARNGDALRSAKEEITelrrtiqSLEIELQSLKKQKA 241

                  ....
gi 1622947863 479 SGER 482
Cdd:pfam00038 242 SLER 245
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
156-473 3.06e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 156 LQTLCEQLRKENEALKAKLdKGLEQRDQAAERLREENLELKKllmsnGNKEGASGQP--GSPKMEGAGKK---------- 223
Cdd:PRK02224  410 AEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLE-----AGKCPECGQPveGSPHVETIEEDrerveeleae 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 224 -AVAGQQQASVTAgKVPEVAALGAAEKKVKMLEQQRSElleVNKQWDQHfrsmkqqyEQKITELRQKLADLQKQVTDLEA 302
Cdd:PRK02224  484 lEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERRED---LEELIAER--------RETIEEKRERAEELRERAAELEA 551
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 303 EREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQTpps 382
Cdd:PRK02224  552 EAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELND--- 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 383 spptafgspegagalLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLSNA 454
Cdd:PRK02224  624 ---------------ERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAVEN 688
                         330       340
                  ....*....|....*....|.
gi 1622947863 455 QLKAFKD--EEKAREANRQQK 473
Cdd:PRK02224  689 ELEELEElrERREALENRVEA 709
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
142-488 3.18e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  142 LASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSngnkegasgQPGSPKMEGAG 221
Cdd:TIGR00618  192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA---------QEEQLKKQQLL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  222 KKAVAGQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSeLLEVNKQWDQHFRSMKQQyEQKITELRQKLADLQKQVTDL 300
Cdd:TIGR00618  263 KQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  301 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTaEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkalEEALSIQTP 380
Cdd:TIGR00618  341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---REQATIDTR 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  381 PSSpptaFGSPEGAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSnaQLKAFK 460
Cdd:TIGR00618  416 TSA----FRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH--LQETRK 488
                          330       340
                   ....*....|....*....|....*...
gi 1622947863  461 DEEKAREANRQQKRKAKASGERYHVEPH 488
Cdd:TIGR00618  489 KAVVLARLLELQEEPCPLCGSCIHPNPA 516
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
242-369 3.35e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 43.18  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALGAAEKKVKMLEQQRSELL-EVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR-KLLLAK 319
Cdd:pfam00529  58 AALDSAEAQLAKAQAQVARLQaELDRL--QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPI 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622947863 320 SKIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam00529 136 GGISRESLVTAG--ALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR 183
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
252-374 3.65e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 252 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 331
Cdd:COG2433   384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622947863 332 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 374
Cdd:COG2433   450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
263-373 3.79e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.02  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 342
Cdd:pfam03938  19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622947863 343 VKYLQDQLSplTRQREYQEKEIQRLNKALEE 373
Cdd:pfam03938  78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
254-375 4.40e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 254 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 333
Cdd:COG0542   413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 334 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 375
Cdd:COG0542   492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
145-466 4.44e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 145 KVHKNEQRTSILqtLCEQLRKENEaLKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMegagkka 224
Cdd:pfam05483 234 EINDKEKQVSLL--LIQITEKENK-MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM------- 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 225 vagQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQH-----------------FRSMKQQYEQKITELR 287
Cdd:pfam05483 304 ---SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvtefeattcsleelLRTEQQRLEKNEDQLK 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 288 QKLADLQKQVTDLEAE---REQKQRDFD--RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL-----------QDQLS 351
Cdd:pfam05483 381 IITMELQKKSSELEEMtkfKNNKEVELEelKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarekeihdlEIQLT 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 352 PLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFgspegagaLLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 431
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--------LLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1622947863 432 NEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 466
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
134-373 5.82e-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: 43.12  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  134 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPg 213
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL- 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  214 SPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQWDQHFRSMK-------------QQYE 280
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAA--EIEELEELIEELESELEALLNERASLEEALAllrseleelseelRELE 907
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  281 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--LLAKSKIEMEETDKEQ--------------------------- 331
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALEnkieddeeearrrlkrlenkikelgpv 987
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622947863  332 -LTA--EAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 373
Cdd:TIGR02168  988 nLAAieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
PTZ00121 PTZ00121
MAEBL; Provisional
134-449 6.52e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  134 RMALEFNRLASKVHKNEQRTSilqtlCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKllmSNGNKEGASGQPG 213
Cdd:PTZ00121  1503 KKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKK---AEEKKKAEEAKKA 1572
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  214 SPKMEGAGKKAVAGQQqasVTAGKVPEVAALGAAEKKVKM-----LEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQ 288
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAeeakkAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKK 1647
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  289 KLADLQK--QVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 366
Cdd:PTZ00121  1648 KAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  367 LNKALEEAlsiqtppsspptafgsPEGAGALLRKQELVTQNELLKQQVK--IFEEDFQRERSDRERMNEEKEELKKQVEK 444
Cdd:PTZ00121  1728 NKIKAEEA----------------KKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791

                   ....*
gi 1622947863  445 LQAQV 449
Cdd:PTZ00121  1792 RRMEV 1796
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
249-445 7.41e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 249 KKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQK------ITELRQKLADLQKQ----VTDLEAERE------------- 305
Cdd:COG1340    71 EKVKELKEERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRqqteVLSPEEEKElvekikelekele 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 306 --QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppss 383
Cdd:COG1340   151 kaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--------- 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622947863 384 pptafgspEGAGALLRKQELVTQNELLKQQVKIFEedfQRERSDRERMNEEKEELKKQVEKL 445
Cdd:COG1340   222 --------QEKADELHEEIIELQKELRELRKELKK---LRKKQRALKREKEKEELEEKAEEI 272
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
242-358 8.22e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALGAAEKKVKMLEQ----QRSELLEVNKQWDQHfRSMKQQYEQKITELRQKLADLQKQVTD-LEAEREQKQRDFDRKLL 316
Cdd:COG1842    16 ALLDKAEDPEKMLDQairdMEEDLVEARQALAQV-IANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERKA 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622947863 317 LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE 358
Cdd:COG1842    95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
246-347 8.28e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.79  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 246 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 325
Cdd:cd16269   202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
                          90       100
                  ....*....|....*....|..
gi 1622947863 326 ETDKEQLTAEAKELRQKVKYLQ 347
Cdd:cd16269   270 ALLEEGFKEQAELLQEEIRSLK 291
PRK11281 PRK11281
mechanosensitive channel MscK;
256-473 9.93e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.21  E-value: 9.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  256 QQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDK 329
Cdd:PRK11281    42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  330 EQL-TAEAKELRQKVKYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FG 389
Cdd:PRK11281   116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKG 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  390 SPEGAGALL--RKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQ 455
Cdd:PRK11281   182 GKVGGKALRpsQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKR 254
                          250
                   ....*....|....*...
gi 1622947863  456 LKAFkdEEKAREANRQQK 473
Cdd:PRK11281   255 LTLS--EKTVQEAQSQDE 270
PTZ00121 PTZ00121
MAEBL; Provisional
161-482 1.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  161 EQLRKENEALKAKLDKGLEQRDQAAERLREENL----ELKKLLMSNG-----------NKEGASGQPGSPKMEGAGKKAV 225
Cdd:PTZ00121  1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEArkaeDAKKAEAARKaeevrkaeelrKAEDARKAEAARKAEEERKAEE 1216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  226 AGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQklADLQKQVTDLEAERE 305
Cdd:PTZ00121  1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK--ADELKKAEEKKKADE 1294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  306 QKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALsiQTPPSSPP 385
Cdd:PTZ00121  1295 AKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE--EKAEAAEK 1371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  386 TAFGSPEGAGALLRKQELVTQNELLKQQVkifEEDFQRERSDRERMNEEK--EELKKQVEKLQAQVTLSNAQLKAFKDEE 463
Cdd:PTZ00121  1372 KKEEAKKKADAAKKKAEEKKKADEAKKKA---EEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADE 1448
                          330       340
                   ....*....|....*....|..
gi 1622947863  464 ---KAREANRQQKRKAKASGER 482
Cdd:PTZ00121  1449 akkKAEEAKKAEEAKKKAEEAK 1470
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
275-482 1.21e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  275 MKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLT 354
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  355 RQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNElLKQQVKIFEEDFQRERSDRERMNEE 434
Cdd:pfam02463  241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-EEELKSELLKLERRKVDDEEKLKES 319
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622947863  435 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 482
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-477 1.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 144 SKVHKNEQRTSILQTLCEQLRKENEALKAKLdKGLEQR-DQAAERLREENLELKKLlmSNGNKEGASGQPGSPKMEGAGK 222
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKiRELEERIEELKKEIEEL--EEKVKELKELKEKAEEYIKLSE 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 223 ---KAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQWDQHFRSMK--QQYEQKITELRQKLADLQ--- 294
Cdd:PRK03918  301 fyeEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELErlk 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 295 KQVTDLEAEREQKQRDfdrklLLAKSKIEMEEtDKEQLTAEAKELRQKVKYLQDQLS--------------PLTRQ---- 356
Cdd:PRK03918  379 KRLTGLTPEKLEKELE-----ELEKAKEEIEE-EISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrELTEEhrke 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 357 --REYQ------EKEIQRLNKALEEALSIQTppsspptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 428
Cdd:PRK03918  453 llEEYTaelkriEKELKEIEEKERKLRKELR------------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL 520
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1622947863 429 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 477
Cdd:PRK03918  521 EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-462 1.36e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 104 NLMLHLQRLETTLSVCAEEPDHSQLFTHLgRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKglEQRDQ 183
Cdd:COG4717   160 ELEEELEELEAELAELQEELEELLEQLSL-ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENEL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 184 AAERLREENLELKKLLMSNG---NKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSe 260
Cdd:COG4717   237 EAAALEERLKEARLLLLIAAallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE- 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 261 lLEvNKQWDQHFRSMKQQYEQKITELR------QKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET--DKEQL 332
Cdd:COG4717   316 -LE-EEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQ 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 333 TAEAKELRQKVKYLQDQLSPLTRQREYQ---------EKEIQRLNKALEEalsiqtppsspptafgspegagalLRKQEL 403
Cdd:COG4717   394 AEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEE------------------------LEEELE 449
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947863 404 VTQNEL--LKQQVKIFEED--FQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:COG4717   450 ELREELaeLEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
248-471 1.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 248 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdrkllLAKSKIEMEET 327
Cdd:COG4372     9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE----------LEQARSELEQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 328 DKE--QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAleealsiqtppsspptafgspegagallrKQELVT 405
Cdd:COG4372    79 EEEleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-----------------------------RQDLEQ 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947863 406 QNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQ 471
Cdd:COG4372   130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
332-452 1.60e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 332 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 410
Cdd:pfam09787  45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622947863 411 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 452
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
282-471 1.86e-03

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.89  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 282 KITELRQKLADLQKQVTDLEAErEQKQRDFDRKLLLAKSKIEMEETDKEQL----TAEAKELRQKVKYLQDQLSPLTRQR 357
Cdd:pfam15619  12 KIKELQNELAELQSKLEELRKE-NRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQEKERDLERKL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 358 EYQEKEIQRLNKALE--EALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQR-----ERSDRER 430
Cdd:pfam15619  91 KEKEAELLRLRDQLKrlEKLSEDK----------------NLAEREELQKKLEQLEAKLEDKDEKIQDlerklELENKSF 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622947863 431 MNEEKEELKKQVEklqAQVTLSNAQLKAFKDEEKAREANRQ 471
Cdd:pfam15619 155 RRQLAAEKKKHKE---AQEEVKILQEEIERLQQKLKEKERE 192
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
262-478 1.95e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  262 LEVNKQwdqhfrSMKQQYEQKIT----ELRQKLADLQKQVTDLEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QLTA 334
Cdd:pfam01576  718 LEVNMQ------ALKAQFERDLQardeQGEEKRRQLVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQIDA 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  335 EAK---ELRQKVKYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQTPPSSPPTAFG---------SP 391
Cdd:pfam01576  789 ANKgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdelAD 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  392 EGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTlsnAQLKAFKDEEKAREANRQ 471
Cdd:pfam01576  869 EIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQLER 945

                   ....*..
gi 1622947863  472 QKRKAKA 478
Cdd:pfam01576  946 QNKELKA 952
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
237-475 2.00e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  237 KVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQyeqkITELRQKLADLQKQVTDLEAEREQKQrdfDRKLL 316
Cdd:pfam01576  126 KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN----LAEEEEKAKSLSKLKNKHEAMISDLE---ERLKK 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  317 LAKSKIEMEETdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspEGAga 396
Cdd:pfam01576  199 EEKGRQELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE------------------ETA-- 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  397 llRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV--TL--SNAQL--------------KA 458
Cdd:pfam01576  258 --QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELedTLdtTAAQQelrskreqevtelkKA 335
                          250
                   ....*....|....*..
gi 1622947863  459 FKDEEKAREANRQQKRK 475
Cdd:pfam01576  336 LEEETRSHEAQLQEMRQ 352
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
277-481 2.11e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.19  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  277 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 346
Cdd:PRK10929    68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  347 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 425
Cdd:PRK10929   136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947863  426 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREANRQQKRKAKASGE 481
Cdd:PRK10929   200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAEQSGD 255
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
154-441 2.75e-03

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: 40.96  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 154 SILQTLCEQL-RKEN--EALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQ 230
Cdd:pfam10174 436 TALTTLEEALsEKERiiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 231 ASvtagkvpevaalgaaekKVKMLE---QQRSEllEVNKQWDQHFRSMKQQYEQKIT-ELRQKLADLQKQVTDLEAEREQ 306
Cdd:pfam10174 516 DS-----------------KLKSLEiavEQKKE--ECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQEVARYKEESGK 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 307 KQRDFDRkLLLAKSKIEMEETDKEQLTAEAKELrqKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPT 386
Cdd:pfam10174 577 AQAEVER-LLGILREVENEKNDKDKKIAELESL--TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863 387 AFGSPEGAGALLR-KQEL-VTQNELLKQQVKIFEED--FQRERSDRERMNEEKEELKKQ 441
Cdd:pfam10174 654 QLQLEELMGALEKtRQELdATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKQE 712
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
278-458 2.87e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 278 QYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKskiemeetDKEQLTAEAKELRQKVKYLQDQLSPLTRQR 357
Cdd:pfam00529  55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQLAQAQIDL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 358 EYQEkeiQRLNKALEEALSIQTppsspptafgspegAGALLRKQE-----LVTQNELLKQQVKIFEEDFQRE-RSDRERM 431
Cdd:pfam00529 127 ARRR---VLAPIGGISRESLVT--------------AGALVAQAQanllaTVAQLDQIYVQITQSAAENQAEvRSELSGA 189
                         170       180
                  ....*....|....*....|....*..
gi 1622947863 432 NEEKEELKKQVEklQAQVTLSNAQLKA 458
Cdd:pfam00529 190 QLQIAEAEAELK--LAKLDLERTEIRA 214
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
254-351 2.95e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 254 LEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 330
Cdd:pfam13863   1 LLEKKREMFLVQLALDA----KREEIERLEELLKQREEELEKKEQELKEDLIKFDkflKENDAKRRRALKKAEEETKLKK 76
                          90       100
                  ....*....|....*....|.
gi 1622947863 331 QLTAEAKELRQKVKYLQDQLS 351
Cdd:pfam13863  77 EKEKEIKKLTAQIEELKSEIS 97
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
312-458 3.23e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.42  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 312 DRKLLLAKSKIEMEETDKE------QLTAEAKELRQKVKYLQDQlspltrQREYQEKEIQRLNKAlEEALSIQtppsspp 385
Cdd:COG1842    23 DPEKMLDQAIRDMEEDLVEarqalaQVIANQKRLERQLEELEAE------AEKWEEKARLALEKG-REDLARE------- 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947863 386 tafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 458
Cdd:COG1842    89 ----------ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
258-461 3.42e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  258 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKQVTDLEAEREQkQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 337
Cdd:COG3096    490 RSQAWQTARELLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLE 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  338 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIF 417
Cdd:COG3096    568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD----------------ALERLREQSGEALADSQEVTAA 631
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622947863  418 -EEDFQRERS---DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 461
Cdd:COG3096    632 mQQLLEREREatvERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
161-475 3.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 161 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgqpgspkmegAGKKAVAGQQQASVTAGKVPE 240
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQL---------------------EEELEELNEQLQAAQAELAQA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 241 VAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKS 320
Cdd:COG4372   100 QEELESLQEEAEELQEELEELQKERQDLEQ----QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE------LAAL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 321 KIEMEETDKEQLTAEAKELRQKVKylqdQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRK 400
Cdd:COG4372   170 EQELQALSEAEAEQALDELLKEAN----RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863 401 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRK 475
Cdd:COG4372   246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
DUF4455 pfam14643
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ...
254-375 3.59e-03

Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.


Pssm-ID: 464231 [Multi-domain]  Cd Length: 469  Bit Score: 40.34  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 254 LEQQRSELLEVNKQWD----QHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLL-------AKSKI 322
Cdd:pfam14643 243 VEEWWASLEALNEQLDqyhdQCMTKLRAEYEEVWQECLARVQKLKQELLDYKVCSEEEAEALVNEEFLplvgklqRDAED 322
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863 323 EMEETDK--EQLtaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL 375
Cdd:pfam14643 323 ELEKLDKflEEL---AKQTEAQSEDLFKFFREAAQLWDVHQTELAKQELELEKKL 374
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-483 3.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 317 LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspegaga 396
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE-------------------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 397 llRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:COG4372    88 --QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165

                  ....*..
gi 1622947863 477 KASGERY 483
Cdd:COG4372   166 LAALEQE 172
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
145-338 4.04e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.09  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 145 KVHKNEQRTSILQTLCEQLRKEnealkakldkgLEQRDQAAERLREENLELKKLLMSNGNKEGASG-QPGSPKMEGAGKK 223
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQ-----------IENKNKNIEELHQENKALKKKGSAENKQLNAYEiKVNKLELELASAK 649
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 224 AVAGQQ----QASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSM-------KQQYEQKITELRQKLA- 291
Cdd:pfam05483 650 QKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMvalmekhKHQYDKIIEERDSELGl 729
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622947863 292 --DLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKE 338
Cdd:pfam05483 730 ykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
242-376 4.25e-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: 39.14  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 242 AALGAAEKKVKMLEQQ----RSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAERE----QKQRDFDR 313
Cdd:COG1579    24 HRLKELPAELAELEDElaalEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLK 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947863 314 KLLLAKSKIEMEETDK-EQLTAEAKELRQKVKYLQDQLSPLTRQRE----YQEKEIQRLNKALEEALS 376
Cdd:COG1579   103 RRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
236-362 4.81e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 39.64  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  236 GKVPE-VAALGAAEKKVKML-EQQRSelleVNKQwdqHFRSMkQQYEQKITELRQKLADLQKQVTDLEAEREQKqRDFDR 313
Cdd:smart00435 245 GNVAEkILAYNRANREVAILcNHQRT----VSKT---HEKSM-EKLQEKIKALKYQLKRLKKMILLFEMISDLK-RKLKS 315
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622947863  314 KLLLAKSKIEME-ETDKEQLTAEAKELRQkVKYLQDQLSPLTRQREYQEK 362
Cdd:smart00435 316 KFERDNEKLDAEvKEKKKEKKKEEKKKKQ-IERLEERIEKLEVQATDKEE 364
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
225-467 5.80e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 39.73  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 225 VAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELlevnKQWDQHFRSMKQqyeqkiTELRQKLAdLQKQVTDLEA-- 302
Cdd:pfam07111  39 VSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQEL----RRLEEEVRLLRE------TSLQQKMR-LEAQAMELDAla 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 303 EREQKQRDFDRKLLLAKSKIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SIQTPP 381
Cdd:pfam07111 108 VAEKAGQAEAEGLRAALAGAEMVRKNLEE--GSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLnSLETKR 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 382 SSPPTAFGSPEGAGALLRKQELVTQNElLKQQVKIFEE-----------DFQRERSDRER---------MNEEKEELKKQ 441
Cdd:pfam07111 186 AGEAKQLAEAQKEAELLRKQLSKTQEE-LEAQVTLVESlrkyvgeqvppEVHSQTWELERqelldtmqhLQEDRADLQAT 264
                         250       260
                  ....*....|....*....|....*.
gi 1622947863 442 VEKLQAQVTlSNAQLKAFKDEEKARE 467
Cdd:pfam07111 265 VELLQVRVQ-SLTHMLALQEEELTRK 289
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
140-475 6.16e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  140 NRLASKVHKNEQRTSILQTLCEQLRKENE--ALKAKLDKGLEQRDQAAERLREEnLELKKLLMSNGNKEGASGQPGSPKM 217
Cdd:TIGR00618  243 AYLTQKREAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLA-AHIKAVTQIEQQAQRIHTELQSKMR 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  218 EGAG---KKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRS--ELLEVNKQWDQHFRSMKQQYE---QKITELRQK 289
Cdd:TIGR00618  322 SRAKllmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTtltQKLQSLCKE 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  290 LADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLTA--------------EAKELRQKVKYLQDQLSPLT- 354
Cdd:TIGR00618  402 LDILQREQATIDT-RTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqceklekiHLQESAQSLKEREQQLQTKEq 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  355 ---RQREYQEKEIQRLNKALEE---------------ALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKI 416
Cdd:TIGR00618  481 ihlQETRKKAVVLARLLELQEEpcplcgscihpnparQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  417 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA-FKDEEKAREANRQQKRK 475
Cdd:TIGR00618  561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKlSEAEDMLACEQHALLRK 620
PRK12705 PRK12705
hypothetical protein; Provisional
222-374 6.36e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.31  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 222 KKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQK 295
Cdd:PRK12705   33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQldaraeKLDNLENQLEEREK 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947863 296 QVTDLEAEREQKQRDFDRKLLlakskiemeetDKEQLTAEakELRQKVkylqdqLSPLtrQREYQEKEIQRLNKALEEA 374
Cdd:PRK12705  113 ALSARELELEELEKQLDNELY-----------RVAGLTPE--QARKLL------LKLL--DAELEEEKAQRVKKIEEEA 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
256-486 6.61e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  256 QQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQV---TDLEAEREQ-------KQRDFDRKLLLAKSKIEME 325
Cdd:pfam01576    8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEmrarlaaRKQELEEILHELESRLEEE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  326 ETDKEQLTAEAKELRQKVKYLQDQLSP--LTRQR----------------------EYQEKEIQRLNKALEEALSIQTpp 381
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEeeAARQKlqlekvtteakikkleedilllEDQNSKLSKERKLLEERISEFT-- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  382 SSPPTAFGSPEGAGALLRKQELVTQNelLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 461
Cdd:pfam01576  166 SNLAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
                          250       260
                   ....*....|....*....|....*
gi 1622947863  462 EEKAREANRQQKRKAKASGERYHVE 486
Cdd:pfam01576  244 ELQAALARLEEETAQKNNALKKIRE 268
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
161-476 6.76e-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: 39.82  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  161 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGN-KEGASGQPGS---------PKMEGAGKKAVAGQQ- 229
Cdd:pfam12128  481 EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAGTllhflrkeaPDWEQSIGKVISPELl 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  230 -----QASVTAGKVPEVAALGAAEKKVKML--------EQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQ 296
Cdd:pfam12128  561 hrtdlDPEVWDGSVGGELNLYGVKLDLKRIdvpewaasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  297 VTD----LEAEREQKQRDFD--RKLLLAKSKIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN 368
Cdd:pfam12128  641 ETFartaLKNARLDLRRLFDekQSEKDKKNKALAERKDSanERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYW 720
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  369 KALEEALSIQTPPSSPPTAfGSPEGAGALLRKQELVTQNEL------------LKQQVKIFE---EDFQRERSD------ 427
Cdd:pfam12128  721 QVVEGALDAQLALLKAAIA-ARRSGAKAELKALETWYKRDLaslgvdpdviakLKREIRTLErkiERIAVRRQEvlryfd 799
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622947863  428 --RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:pfam12128  800 wyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKA 850
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
241-477 7.82e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  241 VAALGAAEKKVKMLEQQRSElleVNKQWDQHfRSMKQQYEQKITELRQKLADLQK---------------QVTDLEAERE 305
Cdd:COG3096    828 VAFAPDPEAELAALRQRRSE---LERELAQH-RAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELD 903
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  306 QKQ------RDFDRKLLLAKSKIEMEETDKEQLtaeaKELRQKVKYLQDQLSPLTRQREYQEKEIQRLnkaleealsiqt 379
Cdd:COG3096    904 AAQeaqafiQQHGKALAQLEPLVAVLQSDPEQF----EQLQADYLQAKEQQRRLKQQIFALSEVVQRR------------ 967
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863  380 ppssppTAFGSPEGAGALLRKQELvtqNELLKQQVkifeedfqrersdrERMNEEKEELKKQVEKLQAQVTLSNAQLKAF 459
Cdd:COG3096    968 ------PHFSYEDAVGLLGENSDL---NEKLRARL--------------EQAEEARREAREQLRQAQAQYSQYNQVLASL 1024
                          250
                   ....*....|....*...
gi 1622947863  460 KdeeKAREANRQQKRKAK 477
Cdd:COG3096   1025 K---SSRDAKQQTLQELE 1039
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
263-466 9.84e-03

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 38.33  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQ- 341
Cdd:COG5074    40 EINQIDNLHKDLLTEVFEEQSRKLRRSLDNFSSQTTDLQRNLKKDIKSAERDGIHLANKQAQAENVRQKFLKLIQDYRIi 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947863 342 KVKYLQDQLSPLTRQR-----EYQEKEIQrlnKALEEALSIQTPPSSPPTAFGSPEGAGALL----RKQELVTQNELLKQ 412
Cdd:COG5074   120 DSNYREEEKEQARRQYiiaqpEATEDEVE---AAINDVNGQQVFSQALLNANRRGEAKTALAevqaRHQEIKKIEKTMAE 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622947863 413 QVKIFeEDFQRERSDRERMneeKEELKKQVEKLQAQVTLSNAQL-KAFKDEEKAR 466
Cdd:COG5074   197 LTQLF-NDMEELVIEQQEN---VDVIDKNVEDAQENVEQGVGHTdKAVKSARAAR 247
 
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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