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Conserved domains on  [gi|1907082466|ref|XP_036012746|]
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sperm-associated antigen 5 isoform X1 [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
58-313 8.28e-10

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 8.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   58 RELTKKLTAKS-RQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRL-------TADLSAQLQILTSTES 129
Cdd:TIGR02168  223 RELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  130 QLKEVRSQHSRCVQDLAVKDELLCQLTQSN---KEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQ 206
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLdelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  207 VAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAK 286
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260
                   ....*....|....*....|....*..
gi 1907082466  287 LKENKAESEIILPSTGSAPAQEHPLSN 313
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQA 489
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-489 2.75e-05

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  189 KEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQE 268
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  269 LRLLAEQLQSLTLFLQAKLKENKAESEIilpstgsapAQEHPLSNDSSISEQTPTAAVDEVpepapvpllgsvKSAFTRV 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEI---------EELEAQIEQLKEELKALREALDEL------------RAELTLL 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  349 ASMASFQPTETPDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLqreicelhSRLQAQEEEHQEALKAKEADMEKLNQ 428
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--------EELEELIEELESELEALLNERASLEE 887
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082466  429 ALCLLRKNEKELLEVIQKQNEKILgqiDKSGQLINLREEVTQLTQSLRRAETETKVLQEAL 489
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
58-313 8.28e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 8.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   58 RELTKKLTAKS-RQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRL-------TADLSAQLQILTSTES 129
Cdd:TIGR02168  223 RELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  130 QLKEVRSQHSRCVQDLAVKDELLCQLTQSN---KEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQ 206
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLdelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  207 VAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAK 286
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260
                   ....*....|....*....|....*..
gi 1907082466  287 LKENKAESEIILPSTGSAPAQEHPLSN 313
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
69-296 1.06e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  69 RQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVK 148
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 149 DELLcqltQSNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRE 228
Cdd:COG1196   315 EERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082466 229 RSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAKLKENKAESEI 296
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-489 2.75e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  189 KEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQE 268
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  269 LRLLAEQLQSLTLFLQAKLKENKAESEIilpstgsapAQEHPLSNDSSISEQTPTAAVDEVpepapvpllgsvKSAFTRV 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEI---------EELEAQIEQLKEELKALREALDEL------------RAELTLL 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  349 ASMASFQPTETPDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLqreicelhSRLQAQEEEHQEALKAKEADMEKLNQ 428
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--------EELEELIEELESELEALLNERASLEE 887
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082466  429 ALCLLRKNEKELLEVIQKQNEKILgqiDKSGQLINLREEVTQLTQSLRRAETETKVLQEAL 489
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
63-279 6.75e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   63 KLTAKSRQALQERDAAIEekkqvvkeveqvsahLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVR--SQHSR 140
Cdd:PRK10929   117 QLLEKSRQAQQEQDRARE---------------ISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQltALQAE 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  141 CVQDLAVKDEL-LCQLTQSNKEqatqwqkeemELKHIQAELLQQQAV-LAKEVQDLRETVEFidEESQVAHRELGQIESQ 218
Cdd:PRK10929   182 SAALKALVDELeLAQLSANNRQ----------ELARLRSELAKKRSQqLDAYLQALRNQLNS--QRQREAERALESTELL 249
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082466  219 LKVTLELLRERSLQCETLRDTVDSL--RAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSL 279
Cdd:PRK10929   250 AEQSGDLPKSIVAQFKINRELSQALnqQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWL 312
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
203-451 1.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 203 EESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKhEKQALEKTHQHSQELRLLAEQLQSLTLF 282
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 283 LQAkLKENKAESEIILPSTGSAPAQEHPLSNDSsiseqtptaavdevpepapvpllgsvksaFTRVASMASFQPTETPDL 362
Cdd:COG4942    99 LEA-QKEELAELLRALYRLGRQPPLALLLSPED-----------------------------FLDAVRRLQYLKYLAPAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 363 EKSLAEMSTVLQELKSLCSLLQESKEEATgVLQREICELHSRLQAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLE 442
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAELE-ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                  ....*....
gi 1907082466 443 VIQKQNEKI 451
Cdd:COG4942   228 LIARLEAEA 236
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
48-205 7.23e-03

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 38.97  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  48 GIWAALLSWSRELTKKLTAKSRQALQerdAAIEEKKQVVKE-VEQVSAHLEDCKGQIEQLKLENSRLTADLSaqlqiltS 126
Cdd:pfam10186  48 GKEEGEQLEDNIGNKKLKLRLLKSEV---AISNERLNEIKDkLDQLRREIAEKKKKIEKLRSSLKQRRSDLE-------S 117
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082466 127 TESQLKEVRSqhsrcvqdlavkdELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLAkevqDLRETVEFIDEES 205
Cdd:pfam10186 118 ASYQLEERRA-------------SQLAKLQNSIKRIKQKWTALHSKTAESRSFLCRELAKLY----GLRQVVKSKNGSS 179
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
58-313 8.28e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 8.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   58 RELTKKLTAKS-RQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRL-------TADLSAQLQILTSTES 129
Cdd:TIGR02168  223 RELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  130 QLKEVRSQHSRCVQDLAVKDELLCQLTQSN---KEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQ 206
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLdelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  207 VAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAK 286
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
                          250       260
                   ....*....|....*....|....*..
gi 1907082466  287 LKENKAESEIILPSTGSAPAQEHPLSN 313
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
69-296 1.06e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  69 RQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVK 148
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 149 DELLcqltQSNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRE 228
Cdd:COG1196   315 EERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082466 229 RSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAKLKENKAESEI 296
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-278 8.77e-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: 55.45  E-value: 8.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466    1 MQEFRGLLQEAQTQLIGLHTEQKELAQQTVSLSSALQQDWTSVQLNYgiwaALLSWSRELTKKLTAKSRQALQERDAAIE 80
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR----KDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   81 EKKQVVKEVEQVSAHLEDCKGQIEQLKLEnsrlTADLSAQLQILtstESQLKEVRSQHSRCVQDLAVKDELLcqltQSNK 160
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKAL---REALDELRAELTLLNEEAANLRERL----ESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  161 EQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTV 240
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907082466  241 DSLRAELASTEAKHEKQALEKthqhsQELRLLAEQLQS 278
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRL-----EGLEVRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-292 1.61e-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: 51.21  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   66 AKSRQALQERDAAIEEKKQVVKEVE----QVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRC 141
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  142 VQDLAVKDELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLA----------KEVQDLRETVEFIDEESQVAHRE 211
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeelkalrEALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  212 LGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTH------QHSQELRLLAEQLQSLTLFLQA 285
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSEELRE 905

                   ....*..
gi 1907082466  286 KLKENKA 292
Cdd:TIGR02168  906 LESKRSE 912
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
61-253 2.08e-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: 50.15  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  61 TKKLTAKSRQALQERDAAIEEKKQVVKEVEQVSAHLEDckgQIEQLKLENSRLTADLSAQLQIL---------TSTESQL 131
Cdd:COG4942    46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQKEELaellralyrLGRQPPL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 132 KEVRSQHSrcVQDLAVKDELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRE 211
Cdd:COG4942   123 ALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907082466 212 LGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAK 253
Cdd:COG4942   201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-489 2.75e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  189 KEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQE 268
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  269 LRLLAEQLQSLTLFLQAKLKENKAESEIilpstgsapAQEHPLSNDSSISEQTPTAAVDEVpepapvpllgsvKSAFTRV 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEI---------EELEAQIEQLKEELKALREALDEL------------RAELTLL 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  349 ASMASFQPTETPDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLqreicelhSRLQAQEEEHQEALKAKEADMEKLNQ 428
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--------EELEELIEELESELEALLNERASLEE 887
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082466  429 ALCLLRKNEKELLEVIQKQNEKILgqiDKSGQLINLREEVTQLTQSLRRAETETKVLQEAL 489
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
70-487 5.14e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  70 QALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILtstesQLKEVRSQHSRCVQDLAVKD 149
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 150 ELLCQLtqsnKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRER 229
Cdd:COG4717   146 ERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 230 slqcetlrdtVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAKLKENKAESEIILPSTGSAPAQEH 309
Cdd:COG4717   222 ----------LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 310 PLSNdssiSEQTPTAAVDEVPEPAPVPLLGS--VKSAFTRVASMASFQPTETPDLEKSLAEMSTVLQELKSLCS--LLQE 385
Cdd:COG4717   292 LLAR----EKASLGKEAEELQALPALEELEEeeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEE 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 386 SKEEATGVLQREICELHSRLQAQEEEHQEALKAKEAdMEKLNQALCLLRKNEKELLEVIQKQN-EKILGQIDKsgQLINL 464
Cdd:COG4717   368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLEALDEEElEEELEELEE--ELEEL 444
                         410       420
                  ....*....|....*....|...
gi 1907082466 465 REEVTQLTQSLRRAETETKVLQE 487
Cdd:COG4717   445 EEELEELREELAELEAELEQLEE 467
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
63-279 6.75e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   63 KLTAKSRQALQERDAAIEekkqvvkeveqvsahLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVR--SQHSR 140
Cdd:PRK10929   117 QLLEKSRQAQQEQDRARE---------------ISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQltALQAE 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  141 CVQDLAVKDEL-LCQLTQSNKEqatqwqkeemELKHIQAELLQQQAV-LAKEVQDLRETVEFidEESQVAHRELGQIESQ 218
Cdd:PRK10929   182 SAALKALVDELeLAQLSANNRQ----------ELARLRSELAKKRSQqLDAYLQALRNQLNS--QRQREAERALESTELL 249
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082466  219 LKVTLELLRERSLQCETLRDTVDSL--RAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSL 279
Cdd:PRK10929   250 AEQSGDLPKSIVAQFKINRELSQALnqQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQWL 312
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-264 3.11e-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: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   78 AIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLkEVRSQHSRcvqdLAVKDELLCQLTQ 157
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAERE----IAELEAELERLDA 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  158 SN------KEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETvefIDEESQVAHRELGQIESQLKVTLELLRERSL 231
Cdd:COG4913    683 SSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAAL 759
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907082466  232 QCETLRDTVDSLRAELASTEAKHEK--QALEKTHQ 264
Cdd:COG4913    760 GDAVERELRENLEERIDALRARLNRaeEELERAMR 794
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
80-576 3.71e-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: 43.50  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   80 EEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRC---VQDLAVKDELL---- 152
Cdd:TIGR00606  405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLegsSDRILELDQELrkae 484
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  153 CQLTQSNKEQATQ-WQKEEMELKHIQAELLQQQAVLAKEVQDL------RETVEFIDEESQVAHRELGQIESQLKVTLEL 225
Cdd:TIGR00606  485 RELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  226 LRERSLQCETLRDTVDSLRAELASTEAKHEKQALE------KTHQHSQELRLLAEQLQSLT--LFLQAKLKENKAESEII 297
Cdd:TIGR00606  565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKElasleqNKNHINNELESKEEQLSSYEdkLFDVCGSQDEESDLERL 644
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  298 LPSTGSAPAQEHPLSNDSSISEQTPTAAVDEVPEPAPV-----PLLGSVKSAFTRVASMASFQPTETPDLEKSLAEMSTV 372
Cdd:TIGR00606  645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  373 LQELKSLCsllqESKEEATGVLQREICELHSRLQAQEEEHQEA---LKAKEADMEKLNQAL-----CLLRKNEKELLEVI 444
Cdd:TIGR00606  725 RDEMLGLA----PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkndIEEQETLLGTIMPEEesakvCLTDVTIMERFQME 800
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  445 QKQNEKILGQIDKSGQLINLREEVTQLTQSLRRAETETKVLQEalEGQLDPSCqlmatnwIQEKvflSQEVSKLRVMFLE 524
Cdd:TIGR00606  801 LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS--KIELNRKL-------IQDQ---QEQIQHLKSKTNE 868
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907082466  525 MKTEKEQLMDKyLSHRHILEENLRRSDTELKKLDDTIQHVYETLLSIPETMK 576
Cdd:TIGR00606  869 LKSEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE 919
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-494 4.49e-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: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   21 EQKELAQQTVSLSSALQQDWTSVQLNYGIWAALLSWSRELTKKLTAKSRQALQERDAAIEEKKQVVK-EVEQVSAHLEDC 99
Cdd:COG4913    249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEaRLDALREELDEL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  100 KGQ--------IEQLKLENSRLTADLSAQLQILT--------------STESQLKEVRSQHSRCVQDLAVKDELLCQLTQ 157
Cdd:COG4913    329 EAQirgnggdrLEQLEREIERLERELEERERRRArleallaalglplpASAEEFAALRAEAAALLEALEEELEALEEALA 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  158 SNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEfideesqvahRELGQIESQLKVTLELLrERSLQCETLR 237
Cdd:COG4913    409 EAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA----------EALGLDEAELPFVGELI-EVRPEEERWR 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  238 DTVDSLRAELAST---EAKHEKQALEKTHQHSQELRLLAEqlqsltlflqaKLKENKAESEIILPSTGSAPA----QEHP 310
Cdd:COG4913    478 GAIERVLGGFALTllvPPEHYAAALRWVNRLHLRGRLVYE-----------RVRTGLPDPERPRLDPDSLAGkldfKPHP 546
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  311 LSN--DSSISEQTPTAAVDEVPE----PAPVPLLGSVKSAFTRVASMASFQPTETP------------------DLEKSL 366
Cdd:COG4913    547 FRAwlEAELGRRFDYVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRYvlgfdnraklaaleaelaELEEEL 626
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  367 AEMSTVLQELKSLCSLLQESKEEATGVLQR-----EICELHSRLQAQEEEHQEALKAKeADMEKLNQALCLLRKNEKELL 441
Cdd:COG4913    627 AEAEERLEALEAELDALQERREALQRLAEYswdeiDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELE 705
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907082466  442 EVIQKQNEKIlGQIDKsgQLINLREEVTQLTQSLRRAETETKV-LQEALEGQLD 494
Cdd:COG4913    706 EELDELKGEI-GRLEK--ELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-478 4.73e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   2 QEFRGLLQEAQTQLIGLHTEQKELAQQ---TVSLSSALQQDWTSVQLNYGIWAALLSWSRELTKKLTAKSRQALQERDAA 78
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  79 IEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVKDELLcqltQS 158
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL----AE 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 159 NKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRD 238
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 239 TVDSLRAELAStEAKHEKQALEKTHQHSQELRLLAEQLQSLT------LFLQAKLKENKAESEIILPSTGSAPAQEHPLS 312
Cdd:COG1196   513 ALLLAGLRGLA-GAVAVLIGVEAAYEAALEAALAAALQNIVVeddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 313 NDSSISEQTP-TAAVDEVPEPAPVPLLGSVKSAFTRVA----SMASFQPTETPDLEKSLAEMSTVLQ----------ELK 377
Cdd:COG1196   592 LARGAIGAAVdLVASDLREADARYYVLGDTLLGRTLVAarleAALRRAVTLAGRLREVTLEGEGGSAggsltggsrrELL 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 378 SLCSLLQESKEEATGVLQREI---CELHSRLQAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLEVIQKQNEKILGQ 454
Cdd:COG1196   672 AALLEAEAELEELAERLAEEElelEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
                         490       500
                  ....*....|....*....|....
gi 1907082466 455 IDKSGQLINLREEVTQLTQSLRRA 478
Cdd:COG1196   752 ALEELPEPPDLEELERELERLERE 775
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
203-451 1.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 203 EESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKhEKQALEKTHQHSQELRLLAEQLQSLTLF 282
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 283 LQAkLKENKAESEIILPSTGSAPAQEHPLSNDSsiseqtptaavdevpepapvpllgsvksaFTRVASMASFQPTETPDL 362
Cdd:COG4942    99 LEA-QKEELAELLRALYRLGRQPPLALLLSPED-----------------------------FLDAVRRLQYLKYLAPAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 363 EKSLAEMSTVLQELKSLCSLLQESKEEATgVLQREICELHSRLQAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLE 442
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAELE-ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                  ....*....
gi 1907082466 443 VIQKQNEKI 451
Cdd:COG4942   228 LIARLEAEA 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
102-296 1.54e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 102 QIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVKDELLCQLTQSNKEQATQWQKEEMELKHIQAELL 181
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 182 QQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEK 261
Cdd:COG4942   101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907082466 262 THQHSQELRLLAEQLQSLTLFLQAKLKENKAESEI 296
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELAAEL 215
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
177-492 1.57e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 177 QAELLQQQAVLAKEVQDLRET------------VEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLR 244
Cdd:COG1196   201 QLEPLERQAEKAERYRELKEElkeleaellllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 245 AELAST-----EAKHEKQALEKTHQHSQELRL-LAEQLQSLTLFLQAKLKENKAESEIIlpstgsapaqehpLSNDSSIS 318
Cdd:COG1196   281 LELEEAqaeeyELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEELEEEL-------------EELEEELE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 319 EQTPTAAVDEVpepapvpLLGSVKSAFTRVASmasfqptetpDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLQREI 398
Cdd:COG1196   348 EAEEELEEAEA-------ELAEAEEALLEAEA----------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 399 cELHSRLQAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLEVIQKQNEKILGQIDKSGQLINLREEVTQLTQSLRRA 478
Cdd:COG1196   411 -ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
                         330
                  ....*....|....
gi 1907082466 479 ETETKVLQEALEGQ 492
Cdd:COG1196   490 AARLLLLLEAEADY 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
72-279 1.78e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466   72 LQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADL---SAQLQILTSTE-----SQLKEVRSQHSRCVQ 143
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelNKKIKDLGEEEqlrvkEKIGELEAEIASLER 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  144 DLAVK------------------DELLCQLTQSNKEQATQ------WQKEEMELKHIQAELLQQQAVLAKEVQDLRETVE 199
Cdd:TIGR02169  309 SIAEKereledaeerlakleaeiDKLLAEIEELEREIEEErkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  200 FIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEkTHQHSQELRLLAEQLQSL 279
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKY 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-483 3.07e-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: 40.81  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  112 RLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVKDELLCQLTQSNKEQATQWQKEEMElkhiQAELLQQQAVLAKEV 191
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  192 QDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQAlEKTHQHSQELRL 271
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-ERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  272 LAEQLQSLtlflqAKLKENKAESEIILpstgsapAQEHplsNDSSISEQTPTAAVDEvpepapvpLLGSVKSAFTRVASM 351
Cdd:TIGR02168  836 TERRLEDL-----EEQIEELSEDIESL-------AAEI---EELEELIEELESELEA--------LLNERASLEEALALL 892
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  352 ASfqptETPDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLQR---EICELHSRLQAQ---EEEHQEALKAK-EADME 424
Cdd:TIGR02168  893 RS----ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEyslTLEEAEALENKiEDDEE 968
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082466  425 KLNQALCLLRKNEKEL-------LEVIQKQNEKilgQIDKSGQLINLREEVTQLTQSLRRAETETK 483
Cdd:TIGR02168  969 EARRRLKRLENKIKELgpvnlaaIEEYEELKER---YDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
406-568 3.78e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 406 QAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLEVIQKQNEKIlgqIDKSGQLINLREEVTQLTQSLRRAETETKVL 485
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 486 QEALEGQLDPSCQLMATNWIQE-----KVFLSQEVSKLRVMFLemktekeQLMDKYLSHRHILEENLRRSDTELKKLDDT 560
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGrqpplALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRADLAELAALRAE 168

                  ....*...
gi 1907082466 561 IQHVYETL 568
Cdd:COG4942   169 LEAERAEL 176
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
54-496 5.61e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  54 LSWSRELTKKLTAKSRQALQERDAA---IEEKKQVVKEVEQVSAHLEDCKGQIEqlklENSRLTADLSAQLQILTSTESQ 130
Cdd:PRK02224  215 LAELDEEIERYEEQREQARETRDEAdevLEEHEERREELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 131 LKEVRSqhsrcvqDLAVKDELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHR 210
Cdd:PRK02224  291 LEEERD-------DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 211 ELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAkhekqALEKTHQHSQELRLLAEQLQSLTLFLQAKLK-- 288
Cdd:PRK02224  364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV-----DLGNAEDFLEELREERDELREREAELEATLRta 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 289 -ENKAESEIILpSTGSAPAQEHPLsndssisEQTPTAAVDEVPEPAPVPLLGSVKSAFTRVASMASfQPTETPDLEKSLA 367
Cdd:PRK02224  439 rERVEEAEALL-EAGKCPECGQPV-------EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAED 509
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466 368 EMSTVLQELKSLCSLLQ------ESKEEATGVLQREICELHSRLQAQEEEHQEALKAKEADMEK---LNQALCLLrKNEK 438
Cdd:PRK02224  510 RIERLEERREDLEELIAerretiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaeLNSKLAEL-KERI 588
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082466 439 ELLEVIQKQNEKILGQIDKSGQLINLREEVTQLTQSLRRAETETKVLQEALEGQLDPS 496
Cdd:PRK02224  589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA 646
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
48-205 7.23e-03

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 38.97  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082466  48 GIWAALLSWSRELTKKLTAKSRQALQerdAAIEEKKQVVKE-VEQVSAHLEDCKGQIEQLKLENSRLTADLSaqlqiltS 126
Cdd:pfam10186  48 GKEEGEQLEDNIGNKKLKLRLLKSEV---AISNERLNEIKDkLDQLRREIAEKKKKIEKLRSSLKQRRSDLE-------S 117
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082466 127 TESQLKEVRSqhsrcvqdlavkdELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLAkevqDLRETVEFIDEES 205
Cdd:pfam10186 118 ASYQLEERRA-------------SQLAKLQNSIKRIKQKWTALHSKTAESRSFLCRELAKLY----GLRQVVKSKNGSS 179
 
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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