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Conserved domains on  [gi|194381832|dbj|BAG64285|]
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unnamed protein product [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 234-320 1.27e-21

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: 87.79  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 234 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 313
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 194381832 314 SQLNRLN 320
Cdd:cd09803   81 RENQELK 87
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-340 1.65e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 189
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   190 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 269
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832   270 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02168  836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 234-320 1.27e-21

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: 87.79  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 234 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 313
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 194381832 314 SQLNRLN 320
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 232-320 1.13e-09

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: 54.99  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  232 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 311
Cdd:pfam16516  12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91


                  ....*....
gi 194381832  312 SQSQLNRLN 320
Cdd:pfam16516  92 LQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-340 1.65e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 189
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   190 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 269
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832   270 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02168  836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-339 6.92e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 6.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 113 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 192
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 268
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832 269 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-339 1.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 179 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 258
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 259 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:COG1196  284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354


                 .
gi 194381832 339 Q 339
Cdd:COG1196  355 E 355
PRK12705 PRK12705
hypothetical protein; Provisional
 133-317 1.34e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 133 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 210
Cdd:PRK12705  23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 211 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 290
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169

                        170       180
                 ....*....|....*....|....*....
gi 194381832 291 ERSDRERLNQE--KEELQQINETSQSQLN 317
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 86-315 2.71e-04

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: 43.19  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   86 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 165
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  166 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 245
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  246 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 315
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-339 4.88e-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: 42.35  E-value: 4.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   179 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 258
Cdd:TIGR02168  173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   259 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:TIGR02168  242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319


                   .
gi 194381832   339 Q 339
Cdd:TIGR02168  320 E 320
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 193-339 7.59e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 272
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194381832   273 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 234-320 1.27e-21

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: 87.79  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 234 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 313
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 194381832 314 SQLNRLN 320
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 232-320 1.13e-09

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: 54.99  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  232 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 311
Cdd:pfam16516  12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91


                  ....*....
gi 194381832  312 SQSQLNRLN 320
Cdd:pfam16516  92 LQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-340 1.65e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 189
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   190 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 269
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832   270 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02168  836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-339 2.95e-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: 55.83  E-value: 2.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   123 QRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRdltRDRLQREEKEKE 202
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   203 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 282
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------LDELRAELTLLNEEAA 820

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 194381832   283 IYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-340 3.00e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 3.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   146 ERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED-----------DRQRDLTRDRLQREEKEKERLNEELHELKE- 213
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEa 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   214 ----ENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFK 289
Cdd:TIGR02169  781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ----------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 194381832   290 KERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-339 6.79e-08

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: 6.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   101 AEPSTRKNLMNSLEQKIRCLEKQ----RKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRK 176
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   177 DDRQRE--DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnKALQDALNIKCSFS 254
Cdd:TIGR02169  774 LHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSI 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   255 EDCLRKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLE 334
Cdd:TIGR02169  853 EKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ....*
gi 194381832   335 KQLKQ 339
Cdd:TIGR02169  931 EELSE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-339 6.92e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 6.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 113 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 192
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 268
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832 269 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 106-310 1.93e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   106 RKNLMNSLEQK---IRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE 182
Cdd:TIGR02168  311 LANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   183 DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEikRLNKALQDAlnikcsfsedclrksr 262
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEEL---------------- 452

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 194381832   263 vEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINE 310
Cdd:TIGR02168  453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 125-339 1.24e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   125 KELLEVNQQWDQQFRSMKElYERKVAELKTKLDAAERFLSTrekdpHQRQRKDDRQREDDRQRDL--TRDRLQREEKEKE 202
Cdd:TIGR02168  232 LRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   203 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 282
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLE 375

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194381832   283 IYEEDFKKERSDR---------------------ERLNQEKEELQQINETSQSQLnrLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR02168  376 ELEEQLETLRSKVaqlelqiaslnneierlearlERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-339 1.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 179 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 258
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 259 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:COG1196  284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354


                 .
gi 194381832 339 Q 339
Cdd:COG1196  355 E 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
114-308 5.74e-06

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: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  114 EQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERkvaeLKTKLDAAERFLSTREKD----PHQRQRkddRQREDDRQR-D 188
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLAEYSWDEidvaSAEREI---AELEAELERlD 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  189 LTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLrksrvefchE 268
Cdd:COG4913   682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 194381832  269 EMRTEmEVLKQQVQIYEEDFKKERSD-RERLNQEKEELQQI 308
Cdd:COG4913   753 ERFAA-ALGDAVERELRENLEERIDAlRARLNRAEEELERA 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 120-339 7.54e-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: 47.45  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 120 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKdphqrqrkddRQREDDRQRDLTRDRLQREEK 199
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALAR----------RIRALEQELAALEAELAELEK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 200 EKERLNEELHELKEEnkllkgkntLANKEKEHYeceikRLNKALQDALNIKCSFSEDCLRKSRVefcheeMRTEMEVLKQ 279
Cdd:COG4942   91 EIAELRAELEAQKEE---------LAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARRE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 280 QVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
158-339 8.73e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 158 AAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIK 237
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 238 RlnKALQDALNIKCSFSEDCLRKSRVefcHEEMRTEMEVLKQQVQIYEEDFKKERSD-----RERLNQEKEELQQInets 312
Cdd:COG4717  134 L--EALEAELAELPERLEELEERLEE---LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEEL---- 204

                        170       180
                 ....*....|....*....|....*..
gi 194381832 313 QSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQ 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 110-329 1.22e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELktklDAAERFLST--REKDPHQRQRKDDRQREDDRQR 187
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEerKRRDKLTEEYAELKEELEDLRA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   188 DL---------TRDRLQREEKEKERLNEELHELKEENKLLKgkntlanKEKEHYECEIKRLNKALQDALNIKCSFSEDcl 258
Cdd:TIGR02169  372 ELeevdkefaeTRDELKDYREKLEKLKREINELKRELDRLQ-------EELQRLSEELADLNAAIAGIEAKINELEEE-- 442

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832   259 rksrvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME 329
Cdd:TIGR02169  443 --------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-325 1.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 113 LEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD 192
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKcsfsedclrksrvefcHEEMRT 272
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----------------EEEEEA 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194381832 273 EMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKA 325
Cdd:COG1196  444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
PRK12705 PRK12705
hypothetical protein; Provisional
 133-317 1.34e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 133 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 210
Cdd:PRK12705  23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 211 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 290
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169

                        170       180
                 ....*....|....*....|....*....
gi 194381832 291 ERSDRERLNQE--KEELQQINETSQSQLN 317
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-339 1.80e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  165 TRE---KDPHQRQRKDDRQReddRQRDL-----TRDRLQREEKEKERLNEELHELKEENKLLKgkntlankekehyecEI 236
Cdd:COG4913   578 TRAgqvKGNGTRHEKDDRRR---IRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEALE---------------AE 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  237 KRLNKALQDALNIKCSFSEDCLRksrvefcHEEMRTEMEVLKQQVQIYEEDfkkeRSDRERLNQEKEELQQINETSQSQL 316
Cdd:COG4913   640 LDALQERREALQRLAEYSWDEID-------VASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEEL 708

                         170       180
                  ....*....|....*....|...
gi 194381832  317 NRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4913   709 DELKGEIGRLEKELEQAEEELDE 731
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-340 2.24e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  111 NSLEQKIRCLEKQRKELLEVNQQWDqqfrsmkelyerKVAELKTKLDAAERFLSTRekDPHQRQRKDD--RQREDDRQRD 188
Cdd:COG4913   238 ERAHEALEDAREQIELLEPIRELAE------------RYAAARERLAELEYLRAAL--RLWFAQRRLEllEAELEELRAE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  189 LTR--DRLQREEKEKERLNEELHELKEEnkllkgKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsedclrksrvefc 266
Cdd:COG4913   304 LARleAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR----------------- 360

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194381832  267 HEEMRTEMEVLKQQVQIYEEDFKKErsdRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:COG4913   361 RARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 86-315 2.71e-04

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: 43.19  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   86 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 165
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  166 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 245
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  246 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 315
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 107-324 4.00e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  107 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLStrEKDPHQRQRKDDRQREDDrq 186
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKK--EKESKISDLEDELNKDDF-- 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  187 rDLTRDRLqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRKSRVEfc 266
Cdd:TIGR04523 553 -ELKKENL---EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKE-- 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194381832  267 HEEMRTEM-------EVLKQQVQIYEEDFKKERSDRERLNQE----KEELQQINETSQSQLNRLNSQIK 324
Cdd:TIGR04523 626 NEKLSSIIknikskkNKLKQEVKQIKETIKEIRNKWPEIIKKikesKTKIDDIIELMKDWLKELSLHYK 694
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-246 4.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 116 KIRCLEKQRKELL-EVNQQWDQQFRSMKELYERKVaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLtRDRL 194
Cdd:COG4717  364 QLEELEQEIAALLaEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL-EEEL 441

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194381832 195 QREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:COG4717  442 EELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
73-315 4.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  73 GKTaSMAHFVQGtsrMIAAESSTEHKECAEPSTRKNLMNSleQKIRCLEKQRKELLEVNQQWDQQfrsmkelyERKVAEL 152
Cdd:COG4717   35 GKS-TLLAFIRA---MLLERLEKEADELFKPQGRKPELNL--KELKELEEELKEAEEKEEEYAEL--------QEELEEL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 153 KTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKE-ENKLLKGKNTLANKEKEH 231
Cdd:COG4717  101 EEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRElEEELEELEAELAELQEEL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 232 YECEIKRLNKALQDAlnikcsfsedclrksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 311
Cdd:COG4717  180 EELLEQLSLATEEEL---------------------QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238


                 ....
gi 194381832 312 SQSQ 315
Cdd:COG4717  239 AALE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-339 4.88e-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: 42.35  E-value: 4.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   179 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 258
Cdd:TIGR02168  173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   259 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:TIGR02168  242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319


                   .
gi 194381832   339 Q 339
Cdd:TIGR02168  320 E 320
COG5022 COG5022
Myosin heavy chain [General function prediction only];
122-335 7.05e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  122 KQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLdaAERFLSTREKDPHQRQRKDDRQREDDRQR-DLTRDRLQREEKE 200
Cdd:COG5022   813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL--IQKFGRSLKAKKRFSLLKKETIYLQSAQRvELAERQLQELKID 890

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  201 KERLNEeLHE--LKEENKLLKGKNTLANKEKEHYECEIKRLNKaLQDALNiKCSFSEDCLRKSRVEFCHEEMRTEMEVLK 278
Cdd:COG5022   891 VKSISS-LKLvnLELESEIIELKKSLSSDLIENLEFKTELIAR-LKKLLN-NIDLEEGPSIEYVKLPELNKLHEVESKLK 967

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 194381832  279 QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLnrlnSQIKACQMEKEKLEK 335
Cdd:COG5022   968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS----KQYGALQESTKQLKE 1020
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 172-339 7.12e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 172 QRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----- 246
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 247 ------------LNIKcSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQS 314
Cdd:COG3883   97 rsggsvsyldvlLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194381832 315 Q-------LNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG3883  176 QqaeqealLAQLSAEEAAAEAQLAELEAELAA 207
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 193-339 7.59e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 272
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194381832   273 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 136-340 8.25e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   136 QQFRSMKELYERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEEN 215
Cdd:TIGR00606  795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   216 KLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE---- 291
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkni 953

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194381832   292 ---RSDRERLNQEKEELQQINEtsQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR00606  954 hgyMKDIENKIQDGKDDYLKQK--ETELNTVNAQLEECEKHQEKINEDMRLM 1003
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-212 1.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  112 SLEQKIRCLEKQRKElleVNQQWDQqfrsmkelYERKVAELKTKLDA-AERFLSTREKDPHQRQRKDDRQREDDRQRDLT 190
Cdd:COG4913   342 QLEREIERLERELEE---RERRRAR--------LEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                          90       100
                  ....*....|....*....|..
gi 194381832  191 RDRLQREEKEKERLNEELHELK 212
Cdd:COG4913   411 EAALRDLRRELRELEAEIASLE 432
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
79-218 1.12e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  79 AHFVQGTS------RMIAAESSTEHKECAEPSTRKNLM-NSLEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAE 151
Cdd:COG2433  370 ARVIRGLSieealeELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIER 445

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194381832 152 LKTKLdaaeRFLSTREKDPHQRQRK-DDRQREDDRqrdLTRdRLQREEKEKERLNEELHELKEENKLL 218
Cdd:COG2433  446 LEREL----SEARSEERREIRKDREiSRLDREIER---LER-ELEEERERIEELKRKLERLKELWKLE 505
PRK11281 PRK11281
mechanosensitive channel MscK;
107-319 1.71e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  107 KNLMNSLEQKIRCL---EKQRKELLEVNQQWDQQFRSMKElYERKVAELKTKLD--AAERF--LSTREKDPHQRQRKDDR 179
Cdd:PRK11281   59 KLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQ-AQAELEALKDDNDeeTRETLstLSLRQLESRLAQTLDQL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  180 QredDRQRDLT---------RDRLQREEKEkerLNEELHELKEENKLLkgKNTLANKEKEHYEcEIKRLNkALQDALNIK 250
Cdd:PRK11281  138 Q---NAQNDLAeynsqlvslQTQPERAQAA---LYANSQRLQQIRNLL--KGGKVGGKALRPS-QRVLLQ-AEQALLNAQ 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194381832  251 CSFSEDCLR---------KSRvefcHEEMRTEMEVLKQQVQIYEEDFKKERsdRERLNQEKEELQQINETSQSQLNRL 319
Cdd:PRK11281  208 NDLQRKSLEgntqlqdllQKQ----RDYLTARIQRLEHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARIQANPL 279
PTZ00121 PTZ00121
MAEBL; Provisional
 91-340 1.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   91 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS---MKELYERKVAELKTKLDAAERFLSTRE 167
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  168 KDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKllKGKNTLANKEKEHYECEikrlnkalqdal 247
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEAEEAKKAE------------ 1705

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  248 NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQvqiyEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQ 327
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                         250
                  ....*....|...
gi 194381832  328 MEKEKLEKQLKQM 340
Cdd:PTZ00121 1782 EEELDEEDEKRRM 1794
tape_meas_lam_C TIGR01541
phage tail tape measure protein, lambda family; This model represents a relatively ...
 112-212 2.19e-03

phage tail tape measure protein, lambda family; This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273681 [Multi-domain]  Cd Length: 332  Bit Score: 39.82  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  112 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDA-------AERFLSTREKDPHQRQRKDDRQREDD 184
Cdd:TIGR01541  28 SRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQLDRfglgdkqRERLDARLQIDRTFRKQQRDLNKAMT 107

                          90       100
                  ....*....|....*....|....*....
gi 194381832  185 RQRDLTRDRLQREE-KEKERLNEELHELK 212
Cdd:TIGR01541 108 AKGLAGSDLYKEQLaAIKASLNEALAELH 136
Cas7_I-C cd09687
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly ...
 176-338 2.63e-03

CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Cst2/DevR family


Pssm-ID: 187818  Cd Length: 302  Bit Score: 39.35  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 176 KDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceikrlnKALQDALNIKCSFSE 255
Cdd:cd09687  158 EVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLSPK----------FVVLGVLNGKNPFFL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 256 DCLrksRVEFCHEEMRTEMEVLKQQVqiyeEDFKKERSDRERLNQEKEELQqiNETSQSQLNRLNSQIKACQMEKEKLEK 335
Cdd:cd09687  228 NSL---RVEEGKSALKIDVELIVTAL----EDFSEKIEDLEHIGLLKGKFA--NELEEIKELLADGGVESEVGIFEEIEK 298


                 ...
gi 194381832 336 QLK 338
Cdd:cd09687  299 AVE 301
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 106-246 2.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 106 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDphQRQRKDDRQREDDR 185
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEA 429

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832 186 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 102-341 3.48e-03

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: 39.62  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  102 EPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE------------------------RKVAELKTKLD 157
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlketiiknnseikdltNQDSVKELIIK 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  158 AAERFLSTREK--DPHQRQRKDDRQREDDRQRDLTRDrlqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECE 235
Cdd:TIGR04523 458 NLDNTRESLETqlKVLSRSINKIKQNLEQKQKELKSK-----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  236 IKRLNKALQDaLNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQ--------------VQIYEEDFKKERSDRERLNQE 301
Cdd:TIGR04523 533 KKEKESKISD-LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTqkslkkkqeekqelIDQKEKEKKDLIKEIEEKEKK 611

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 194381832  302 KEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMY 341
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 106-246 3.89e-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: 39.32  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  106 RKNLMNSLEQKIRCLeKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRkddrqreddr 185
Cdd:pfam05483 519 QEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK---------- 587

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832  186 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 181-339 4.11e-03

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: 39.23  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  181 REDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRK 260
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-KLELLLSNLKKKIQK 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  261 srvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQ-QINETSQSQlNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR04523 213 ------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtQLNQLKDEQ-NKIKKQLSEKQKELEQNNKKIKE 285
PTZ00121 PTZ00121
MAEBL; Provisional
 91-338 5.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   91 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKEllEVNQQWDQQFRSMKELYE-----------RKVAELKTKLDAA 159
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKaaaakkkadeaKKKAEEKKKADEA 1436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  160 ERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEK-------ERLNEELHELKEENKLLKGKNTLANKEKEHY 232
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  233 ECEIKRLNKALQDALNIKcsfSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS 312
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                         250       260
                  ....*....|....*....|....*.
gi 194381832  313 QSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAK 1619
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
125-340 5.26e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 125 KELLEVNQQwdqQFRSMKELYERKVAELKTKLDAAErflstrekdphqRQRKDDRQRED----DRQRDLTRDRLqreeke 200
Cdd:COG3206  163 EQNLELRRE---EARKALEFLEEQLPELRKELEEAE------------AALEEFRQKNGlvdlSEEAKLLLQQL------ 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832 201 kERLNEELHELKEENKLLKGKntlankekehyeceIKRLNKALQDALNIKCSFSEDCLRksrvefchEEMRTEMEVLKQQ 280
Cdd:COG3206  222 -SELESQLAEARAELAEAEAR--------------LAALRAQLGSGPDALPELLQSPVI--------QQLRAQLAELEAE 278

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194381832 281 VQIYEEDFKKERSDRERLNQEKEEL-QQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:COG3206  279 LAELSARYTPNHPDVIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQL 339
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-335 7.15e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   108 NLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERflstrekdphQRQRKDDRQREDDRQR 187
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELES----------ELEALLNERASLEEAL 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832   188 DLTRDRLQREEKEKERLNEELHELKEEnklLKGKNTLANKEKEhyeceikRLNKALQDALNIKCSFSEdclrksrvefch 267
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLEL-------RLEGLEVRIDNLQERLSE------------ 947

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194381832   268 eEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS-------QSQLNRLNSQIKACQMEKEKLEK 335
Cdd:TIGR02168  948 -EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieeyeelKERYDFLTAQKEDLTEAKETLEE 1021
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 268-341 8.54e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 8.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194381832 268 EEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME----KEKLEKQLKQMY 341
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERARALY 96
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 112-338 9.05e-03

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: 38.08  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  112 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTR 191
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  192 DRLQREEKEKERLNEElhelKEENKLLKGKNTLANKEKEHYECE------IKRLNKALQDALNIKCSFSEDCLRKSRVEF 265
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQ----KEQDWNKELKSELKNQEKKLEEIQnqisqnNKIISQLNEQISQLKKELTNSESENSEKQR 363

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194381832  266 CHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINEtsqsqlnRLNSQIKACQMEKEKLEKQLK 338
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-------QKDEQIKKLQQEKELLEKEIE 429
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 125-319 9.95e-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: 38.01  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  125 KELLEvnqqwdqQFRSMKELYERkVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERL 204
Cdd:COG3096   498 RELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194381832  205 NEELHELKEENKLLKgkntlanKEKEHYECEIKRLNK------ALQDALNIKCsfsedclrksrvEFCHEEMRTEMEVLK 278
Cdd:COG3096   570 EEQAAEAVEQRSELR-------QQLEQLRARIKELAArapawlAAQDALERLR------------EQSGEALADSQEVTA 630

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 194381832  279 --QQVQIYEEDFKKERSD----RERLNQEKEELQQINETSQSQLNRL 319
Cdd:COG3096   631 amQQLLEREREATVERDElaarKQALESQIERLSQPGGAEDPRLLAL 677
 
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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