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Conserved domains on  [gi|119625670|gb|EAX05265|]
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TNFAIP3 interacting protein 3, isoform CRA_c [Homo sapiens]

Protein Classification

Graphical summary

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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) ...
 157-243 6.23e-22

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: 88.56  E-value: 6.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 157 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 236
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 119625670 237 SQLNRLN 243
Cdd:cd09803   81 RENQELK 87
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-263 1.53e-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: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    33 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 112
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   113 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 192
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670   193 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
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) ...
 157-243 6.23e-22

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: 88.56  E-value: 6.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 157 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 236
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 119625670 237 SQLNRLN 243
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 155-243 8.22e-10

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: 55.38  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  155 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 234
Cdd:pfam16516  12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91


                  ....*....
gi 119625670  235 SQSQLNRLN 243
Cdd:pfam16516  92 LQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-263 1.53e-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: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    33 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 112
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   113 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 192
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670   193 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
Cdd:TIGR02168  836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-262 9.06e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  36 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 115
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 116 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 191
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670 192 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-262 2.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 102 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 181
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 182 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 261
Cdd:COG1196  284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354


                 .
gi 119625670 262 Q 262
Cdd:COG1196  355 E 355
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-238 6.99e-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: 44.73  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    9 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 88
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   89 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 168
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  169 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 238
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
PRK12705 PRK12705
hypothetical protein; Provisional
 56-240 1.26e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.54  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  56 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 133
Cdd:PRK12705  23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 134 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 213
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169

                        170       180
                 ....*....|....*....|....*....
gi 119625670 214 ERSDRERLNQE--KEELQQINETSQSQLN 240
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-262 4.85e-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: 41.97  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   102 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 181
Cdd:TIGR02168  173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   182 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 261
Cdd:TIGR02168  242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319


                   .
gi 119625670   262 Q 262
Cdd:TIGR02168  320 E 320
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 116-262 6.00e-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: 6.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   116 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 195
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119625670   196 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
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) ...
 157-243 6.23e-22

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: 88.56  E-value: 6.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 157 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 236
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 119625670 237 SQLNRLN 243
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 155-243 8.22e-10

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: 55.38  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  155 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 234
Cdd:pfam16516  12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91


                  ....*....
gi 119625670  235 SQSQLNRLN 243
Cdd:pfam16516  92 LQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-263 1.53e-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: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    33 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 112
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   113 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 192
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670   193 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
Cdd:TIGR02168  836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 69-263 1.95e-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: 56.23  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    69 ERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED-----------DRQRDLTRDRLQREEKEKERLNEELHELKE- 136
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEa 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   137 ----ENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFK 212
Cdd:TIGR02169  781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ----------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 119625670   213 KERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-262 2.63e-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: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    46 QRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRdltRDRLQREEKEKE 125
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   126 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 205
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------LDELRAELTLLNEEAA 820

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119625670   206 IYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 24-262 4.50e-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: 55.07  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    24 AEPSTRKNLMNSLEQKIRCLEKQ----RKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRK 99
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   100 DDRQRE--DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnKALQDALNIKCSFS 177
Cdd:TIGR02169  774 LHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSI 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   178 EDCLRKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLE 257
Cdd:TIGR02169  853 EKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ....*
gi 119625670   258 KQLKQ 262
Cdd:TIGR02169  931 EELSE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-262 9.06e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  36 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 115
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 116 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 191
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670 192 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-233 1.98e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    29 RKNLMNSLEQK---IRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE 105
Cdd:TIGR02168  311 LANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   106 DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEikRLNKALQDAlnikcsfsedclrksr 185
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEEL---------------- 452

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 119625670   186 vEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINE 233
Cdd:TIGR02168  453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-262 1.32e-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: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    48 KELLEVNQQWDQQFRSMKElYERKVAELKTKLDAAERFLSTrekdpHQRQRKDDRQREDDRQRDL--TRDRLQREEKEKE 125
Cdd:TIGR02168  232 LRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   126 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 205
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLE 375

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625670   206 IYEEDFKKERSDR---------------------ERLNQEKEELQQINETSQSQLnrLNSQIKACQMEKEKLEKQLKQ 262
Cdd:TIGR02168  376 ELEEQLETLRSKVaqlelqiaslnneierlearlERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-262 2.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 102 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 181
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 182 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 261
Cdd:COG1196  284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354


                 .
gi 119625670 262 Q 262
Cdd:COG1196  355 E 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-231 1.23e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   37 EQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERkvaeLKTKLDAAERFLSTREKD----PHQRQRkddRQREDDRQR-D 111
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLAEYSWDEidvaSAEREI---AELEAELERlD 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  112 LTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLrksrvefchE 191
Cdd:COG4913   682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 119625670  192 EMRTEmEVLKQQVQIYEEDFKKERSD-RERLNQEKEELQQI 231
Cdd:COG4913   753 ERFAA-ALGDAVERELRENLEERIDAlRARLNRAEEELERA 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-262 3.94e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  43 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKdphqrqrkddRQREDDRQRDLTRDRLQREEK 122
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALAR----------RIRALEQELAALEAELAELEK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 123 EKERLNEELHELKEEnkllkgkntLANKEKEHYeceikRLNKALQDALNIKCSFSEDCLRKSRVefcheeMRTEMEVLKQ 202
Cdd:COG4942   91 EIAELRAELEAQKEE---------LAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARRE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 203 QVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-247 6.00e-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: 45.01  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   30 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLStrEKDPHQRQRKDDRQREDDrq 109
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKK--EKESKISDLEDELNKDDF-- 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  110 rDLTRDRLqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRKSRVEfc 189
Cdd:TIGR04523 553 -ELKKENL---EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKE-- 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625670  190 HEEMRTEM-------EVLKQQVQIYEEDFKKERSDRERLNQE----KEELQQINETSQSQLNRLNSQIK 247
Cdd:TIGR04523 626 NEKLSSIIknikskkNKLKQEVKQIKETIKEIRNKWPEIIKKikesKTKIDDIIELMKDWLKELSLHYK 694
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-238 6.99e-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: 44.73  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    9 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 88
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   89 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 168
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  169 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 238
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-252 7.98e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    33 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELktklDAAERFLST--REKDPHQRQRKDDRQREDDRQR 110
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEerKRRDKLTEEYAELKEELEDLRA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   111 DL---------TRDRLQREEKEKERLNEELHELKEENKLLKgkntlanKEKEHYECEIKRLNKALQDALNIKCSFSEDcl 181
Cdd:TIGR02169  372 ELeevdkefaeTRDELKDYREKLEKLKREINELKRELDRLQ-------EELQRLSEELADLNAAIAGIEAKINELEEE-- 442

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670   182 rksrvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME 252
Cdd:TIGR02169  443 --------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
PRK12705 PRK12705
hypothetical protein; Provisional
 56-240 1.26e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.54  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  56 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 133
Cdd:PRK12705  23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 134 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 213
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169

                        170       180
                 ....*....|....*....|....*....
gi 119625670 214 ERSDRERLNQE--KEELQQINETSQSQLN 240
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-248 1.56e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  36 LEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD 115
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 116 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKcsfsedclrksrvefcHEEMRT 195
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----------------EEEEEA 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119625670 196 EMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKA 248
Cdd:COG1196  444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-262 2.21e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  81 AAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIK 160
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 161 RlnKALQDALNIKCSFSEDCLRKSRVefcHEEMRTEMEVLKQQVQIYEEDFKKERSD-----RERLNQEKEELQQInets 235
Cdd:COG4717  134 L--EALEAELAELPERLEELEERLEE---LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEEL---- 204

                        170       180
                 ....*....|....*....|....*..
gi 119625670 236 QSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQ 231
PTZ00121 PTZ00121
MAEBL; Provisional
 14-263 2.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   14 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS---MKELYERKVAELKTKLDAAERFLSTRE 90
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   91 KDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKllKGKNTLANKEKEHYECEikrlnkalqdal 170
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEAEEAKKAE------------ 1705

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  171 NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQvqiyEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQ 250
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                         250
                  ....*....|...
gi 119625670  251 MEKEKLEKQLKQM 263
Cdd:PTZ00121 1782 EEELDEEDEKRRM 1794
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 59-263 2.84e-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: 43.11  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    59 QQFRSMKELYERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEEN 138
Cdd:TIGR00606  795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   139 KLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE---- 214
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkni 953

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119625670   215 ---RSDRERLNQEKEELQQINEtsQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
Cdd:TIGR00606  954 hgyMKDIENKIQDGKDDYLKQK--ETELNTVNAQLEECEKHQEKINEDMRLM 1003
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 44-262 3.78e-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: 42.42  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   44 EKQRKELLEVNQQwdQQFRSMKELYERKVaELKTKLDAAER-----------FLSTREKDPHQRQRKDDRQREDDRQRDL 112
Cdd:pfam17380 286 ERQQQEKFEKMEQ--ERLRQEKEEKAREV-ERRRKLEEAEKarqaemdrqaaIYAEQERMAMERERELERIRQEERKREL 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  113 TRDRLQREEKEKERLNE-ELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHE 191
Cdd:pfam17380 363 ERIRQEEIAMEISRMRElERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625670  192 EMRTEMEVLK-------QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:pfam17380 443 ERAREMERVRleeqerqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-262 3.96e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   91 KDPHQRQRKDDRQReddRQRDL-----TRDRLQREEKEKERLNEELHELKEENKLLKgkntlankekehyecEIKRLNKA 165
Cdd:COG4913   584 KGNGTRHEKDDRRR---IRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEALE---------------AELDALQE 645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  166 LQDALNIKCSFSEDCLRksrvefcHEEMRTEMEVLKQQVQIYEEDfkkeRSDRERLNQEKEELQQINETSQSQLNRLNSQ 245
Cdd:COG4913   646 RREALQRLAEYSWDEID-------VASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGE 714

                         170
                  ....*....|....*..
gi 119625670  246 IKACQMEKEKLEKQLKQ 262
Cdd:COG4913   715 IGRLEKELEQAEEELDE 731
COG5022 COG5022
Myosin heavy chain [General function prediction only];
45-258 4.65e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.37  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   45 KQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLdaAERFLSTREKDPHQRQRKDDRQREDDRQR-DLTRDRLQREEKE 123
Cdd:COG5022   813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL--IQKFGRSLKAKKRFSLLKKETIYLQSAQRvELAERQLQELKID 890

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  124 KERLNEeLHE--LKEENKLLKGKNTLANKEKEHYECEIKRLNKaLQDALNiKCSFSEDCLRKSRVEFCHEEMRTEMEVLK 201
Cdd:COG5022   891 VKSISS-LKLvnLELESEIIELKKSLSSDLIENLEFKTELIAR-LKKLLN-NIDLEEGPSIEYVKLPELNKLHEVESKLK 967

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119625670  202 QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLnrlnSQIKACQMEKEKLEK 258
Cdd:COG5022   968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS----KQYGALQESTKQLKE 1020
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-262 4.85e-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: 41.97  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   102 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 181
Cdd:TIGR02168  173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   182 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 261
Cdd:TIGR02168  242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319


                   .
gi 119625670   262 Q 262
Cdd:TIGR02168  320 E 320
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
34-263 5.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   34 NSLEQKIRCLEKQRKELLEVNQQWDqqfrsmkelyerKVAELKTKLDAAERFLSTRekDPHQRQRK----DDRQREDDRQ 109
Cdd:COG4913   238 ERAHEALEDAREQIELLEPIRELAE------------RYAAARERLAELEYLRAAL--RLWFAQRRlellEAELEELRAE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  110 RDLTRDRLQREEKEKERLNEELHELKEEnkllkgKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsedclrksrvefc 189
Cdd:COG4913   304 LARLEAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR----------------- 360

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625670  190 HEEMRTEMEVLKQQVQIYEEDFKKErsdRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 263
Cdd:COG4913   361 RARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-264 5.83e-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: 41.93  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   25 EPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE------------------------RKVAELKTKLD 80
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlketiiknnseikdltNQDSVKELIIK 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   81 AAERFLSTREK--DPHQRQRKDDRQREDDRQRDLTRDrlqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECE 158
Cdd:TIGR04523 458 NLDNTRESLETqlKVLSRSINKIKQNLEQKQKELKSK-----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  159 IKRLNKALQDaLNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQ--------------VQIYEEDFKKERSDRERLNQE 224
Cdd:TIGR04523 533 KKEKESKISD-LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTqkslkkkqeekqelIDQKEKEKKDLIKEIEEKEKK 611

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 119625670  225 KEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMY 264
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 116-262 6.00e-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: 6.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   116 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 195
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119625670   196 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
PTZ00121 PTZ00121
MAEBL; Provisional
 14-261 7.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   14 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKEllEVNQQWDQQFRSMKELYE-----------RKVAELKTKLDAA 82
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKaaaakkkadeaKKKAEEKKKADEA 1436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   83 ERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEK-------ERLNEELHELKEENKLLKGKNTLANKEKEHY 155
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  156 ECEIKRLNKALQDALNIKcsfSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS 235
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                         250       260
                  ....*....|....*....|....*.
gi 119625670  236 QSQLNRLNSQIKACQMEKEKLEKQLK 261
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAK 1619
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-169 9.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 9.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  39 KIRCLEKQRKELL-EVNQQWDQQFRSMKELYERKVaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLtRDRL 117
Cdd:COG4717  364 QLEELEQEIAALLaEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL-EEEL 441

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119625670 118 QREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 169
Cdd:COG4717  442 EELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-141 9.64e-04

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: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   2 AHFVQGTS------RMIAAESSTEHKECAEPSTRKNLM-NSLEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAE 74
Cdd:COG2433  370 ARVIRGLSieealeELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIER 445

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625670  75 LKTKLdaaeRFLSTREKDPHQRQRK-DDRQREDDRqrdLTRdRLQREEKEKERLNEELHELKEENKLL 141
Cdd:COG2433  446 LEREL----SEARSEERREIRKDREiSRLDREIER---LER-ELEEERERIEELKRKLERLKELWKLE 505
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-262 1.01e-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: 41.16  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  104 REDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRK 183
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-KLELLLSNLKKKIQK 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  184 srvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQ-QINETSQSQlNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:TIGR04523 213 ------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtQLNQLKDEQ-NKIKKQLSEKQKELEQNNKKIKE 285
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 29-169 1.16e-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: 40.86  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   29 RKNLMNSLEQKIRCLeKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRkddrqreddr 108
Cdd:pfam05483 519 QEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK---------- 587

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670  109 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 169
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
35-135 1.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   35 SLEQKIRCLEKQRKElleVNQQWDQqfrsmkelYERKVAELKTKLDA-AERFLSTREKDPHQRQRKDDRQREDDRQRDLT 113
Cdd:COG4913   342 QLEREIERLERELEE---RERRRAR--------LEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                          90       100
                  ....*....|....*....|..
gi 119625670  114 RDRLQREEKEKERLNEELHELK 135
Cdd:COG4913   411 EAALRDLRRELRELEAEIASLE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
38-238 1.80e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  38 QKIRCLEKQRKELLEVNQQWDQQfrsmkelyERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRL 117
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAEL--------QEELEELEEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAEL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 118 QREEKEKERLNEELHELKE-ENKLLKGKNTLANKEKEHYECEIKRLNKALQDAlnikcsfsedclrksrvefchEEMRTE 196
Cdd:COG4717  142 AELPERLEELEERLEELRElEEELEELEAELAELQEELEELLEQLSLATEEEL---------------------QDLAEE 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119625670 197 MEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQ 238
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PTZ00121 PTZ00121
MAEBL; Provisional
 14-262 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 119625670   14 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyeRKVAELKTKLDAAERFLSTREKDp 93
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKAD- 1525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   94 HQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIK 173
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  174 CSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINET---SQSQLNRLNSQIKACQ 250
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEeakKAEEDKKKAEEAKKAE 1684

                         250
                  ....*....|..
gi 119625670  251 MEKEKLEKQLKQ 262
Cdd:PTZ00121 1685 EDEKKAAEALKK 1696
Cas7_I-C cd09687
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly ...
 99-261 2.11e-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: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  99 KDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceikrlnKALQDALNIKCSFSE 178
Cdd:cd09687  158 EVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLSPK----------FVVLGVLNGKNPFFL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 179 DCLrksRVEFCHEEMRTEMEVLKQQVqiyeEDFKKERSDRERLNQEKEELQqiNETSQSQLNRLNSQIKACQMEKEKLEK 258
Cdd:cd09687  228 NSL---RVEEGKSALKIDVELIVTAL----EDFSEKIEDLEHIGLLKGKFA--NELEEIKELLADGGVESEVGIFEEIEK 298


                 ...
gi 119625670 259 QLK 261
Cdd:cd09687  299 AVE 301
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 35-261 2.46e-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: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   35 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTR 114
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  115 DRLQREEKEKERLNEElhelKEENKLLKGKNTLANKEKEHYECE------IKRLNKALQDALNIKCSFSEDCLRKSRVEF 188
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQ----KEQDWNKELKSELKNQEKKLEEIQnqisqnNKIISQLNEQISQLKKELTNSESENSEKQR 363

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625670  189 CHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINEtsqsqlnRLNSQIKACQMEKEKLEKQLK 261
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-------QKDEQIKKLQQEKELLEKEIE 429
tape_meas_lam_C TIGR01541
phage tail tape measure protein, lambda family; This model represents a relatively ...
 35-135 2.59e-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: 39.44  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   35 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDA-------AERFLSTREKDPHQRQRKDDRQREDD 107
Cdd:TIGR01541  28 SRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQLDRfglgdkqRERLDARLQIDRTFRKQQRDLNKAMT 107

                          90       100
                  ....*....|....*....|....*....
gi 119625670  108 RQRDLTRDRLQREE-KEKERLNEELHELK 135
Cdd:TIGR01541 108 AKGLAGSDLYKEQLaAIKASLNEALAELH 136
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-169 3.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  29 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDphQRQRKDDRQREDDR 108
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEA 429

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670 109 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 169
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-262 3.70e-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: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   43 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAErflSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEK 122
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL-NEQISQLKKELTNSE---SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  123 EKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnkaLQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQ 202
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL---KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119625670  203 QVQIYEEDFKKERSDRERLNQE-----KEELQQINETSQS--QLNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEKKELeeKVKDLTKKISSLKEKIEKLESEKKE 535
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 95-262 3.89e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  95 QRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----- 169
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 170 ------------LNIKcSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQS 237
Cdd:COG3883   97 rsggsvsyldvlLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119625670 238 Q-------LNRLNSQIKACQMEKEKLEKQLKQ 262
Cdd:COG3883  176 QqaeqealLAQLSAEEAAAEAQLAELEAELAA 207
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-228 4.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  10 RMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEvnqqwdqqfrSMKELyERKVAELKTKLdaaeRFLSTR 89
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE----------KIREL-EERIEELKKEI----EELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  90 EKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLN------ 163
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerh 361

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625670 164 KALQDALNIKCSFSEdcLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEEL 228
Cdd:PRK03918 362 ELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 18-221 6.29e-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: 38.65  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   18 TEHKEC--AEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKElyerKVAELKTKLDAAERFLSTREKDPHQ 95
Cdd:pfam10174 372 TEEKSTlaGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE----RVKSLQTDSSNTDTALTTLEEALSE 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   96 RQRKDDRQREddrQRDltRDRLQREEkEKERLNEELHELKEENKLLKG----KNTLANKEKEHYECE----IKRLNKALQ 167
Cdd:pfam10174 448 KERIIERLKE---QRE--REDRERLE-ELESLKKENKDLKEKVSALQPelteKESSLIDLKEHASSLassgLKKDSKLKS 521

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625670  168 DALNIK-----CSFSEDCLRKSR----VEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERL 221
Cdd:pfam10174 522 LEIAVEqkkeeCSKLENQLKKAHnaeeAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-229 6.97e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    33 MNSLEQKIRCLEKQRKELLEVNQQWDQQfrsmKELYERKVAELKTKLDAAERflstrEKDPHQRQRKDDRQREDDRQRDl 112
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEE-----ELEELEAALRDLESRLGDLKKE- 890

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   113 tRDRLQRE----EKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsEDClrKSRVEF 188
Cdd:TIGR02169  891 -RDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDV--QAELQR 962

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119625670   189 CHEEMRTEMEVLKQQVQIYEE---DFKKERSDRERLNQEKEELQ 229
Cdd:TIGR02169  963 VEEEIRALEPVNMLAIQEYEEvlkRLDELKEKRAKLEEERKAIL 1006
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-258 7.41e-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: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670    35 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLStrekdphQRQRKDDRQREDDRQRDLTR 114
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-------ELEALLNERASLEEALALLR 893

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670   115 DRLQREEKEKERLNEELHELKEEnklLKGKNTLANKEKEhyeceikRLNKALQDALNIKCSFSEdclrksrvefcheEMR 194
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRE---LEELREKLAQLEL-------RLEGLEVRIDNLQERLSE-------------EYS 950

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625670   195 TEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS-------QSQLNRLNSQIKACQMEKEKLEK 258
Cdd:TIGR02168  951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieeyeelKERYDFLTAQKEDLTEAKETLEE 1021
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
29-263 8.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670  29 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS--MKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE- 105
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEk 529

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 106 --------DDRQRDLTRD--RLQREEKEKERLNEELHELKEENKLLKGK-NTLANKEKEHYECEIKRLNKALQDALNIKC 174
Cdd:PRK03918 530 lkekliklKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKD 609

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625670 175 SFSEDCLRKSRVEFCHEEM----------RTEMEVLKQQVQIYEEDFKKErsDRERLNQEKEELQQINETSQSQLNRLNS 244
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdkafeelaetEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEK 687

                        250
                 ....*....|....*....
gi 119625670 245 QIKACQMEKEKLEKQLKQM 263
Cdd:PRK03918 688 RREEIKKTLEKLKEELEER 706
 
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.
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