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Conserved domains on  [gi|2067662260|ref|NP_001382467|]
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protein BCAP isoform o [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
170-426 1.51e-08

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  170 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 249
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  250 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 327
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  328 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 407
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662260  408 KILDLETELRKKNEEQNQL 426
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
62-268 5.22e-04

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  62 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 141
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 142 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 207
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662260 208 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 268
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
170-426 1.51e-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: 57.00  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  170 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 249
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  250 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 327
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  328 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 407
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662260  408 KILDLETELRKKNEEQNQL 426
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-426 7.48e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 7.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  250 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 317
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  318 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 391
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662260  392 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 426
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
PRK11637 PRK11637
AmiB activator; Provisional
248-421 3.15e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 248 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 317
Cdd:PRK11637   59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 318 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 377
Cdd:PRK11637  139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2067662260 378 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 421
Cdd:PRK11637  217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
62-268 5.22e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  62 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 141
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 142 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 207
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662260 208 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 268
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-273 7.19e-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: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260    1 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 73
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   74 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 150
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  151 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 230
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2067662260  231 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 273
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
203-435 1.68e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 203 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 280
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 281 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 355
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 356 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 420
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
                         250
                  ....*....|....*
gi 2067662260 421 EEQNQLVCKMNSDPE 435
Cdd:pfam05667 475 ELYKQLVAEYERLPK 489
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
170-426 1.51e-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: 57.00  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  170 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 249
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  250 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 327
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  328 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 407
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662260  408 KILDLETELRKKNEEQNQL 426
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
123-427 7.09e-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: 51.60  E-value: 7.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  123 IEKTELEVQIETMKKQIINLLEDLKKMEDhgknSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 202
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  203 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHE 282
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAELEELEAELEELESRLEE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  283 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKCENLQQKLEQMDAENKELEKKLANQEECLKHS 362
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662260  363 NLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilDLETELRKKNEEQNQLV 427
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-426 7.48e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 7.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  250 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 317
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  318 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 391
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662260  392 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 426
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
63-398 1.23e-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: 47.74  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   63 EASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSET-------ISASNAWKSHYEKIVIEKTELEVQIETM 135
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarlEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  136 KKQIINLLEDLKKMEDHGKNSCEEIlrkvhsieyenETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEM 215
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI-----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  216 YKTQVQKLQEAAEIVKSRCENLlhknnqitktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCA 295
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESL-----------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  296 DQEHTIRELQGQVDGNHNLLTKLSLEEENclIQLKCENLQQKL---EQMDAEN-KELEKKLANQEECLKHS--------- 362
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEG--LEVRIDNLQERLseeYSLTLEEaEALENKIEDDEEEARRRlkrlenkik 982
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2067662260  363 -----NL----KFKEKSAEYTALARQLEaALEEGRQKVAEEIEKM 398
Cdd:TIGR02168  983 elgpvNLaaieEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEI 1026
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
264-426 4.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 264 KELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDA 343
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 344 ENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmSSRESALQIKILDLETELRKKNEEQ 423
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEEL 423

                  ...
gi 2067662260 424 NQL 426
Cdd:COG1196   424 EEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
71-356 7.85e-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: 45.05  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   71 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKme 150
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-- 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  151 dhgknsceeilrkvhsIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 230
Cdd:TIGR02168  321 ----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  231 KSRCENLLHKNNQITKTknknVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQVDG 310
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER 458
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2067662260  311 NHNLLTKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANQE 356
Cdd:TIGR02168  459 LEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
124-423 8.04e-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: 45.06  E-value: 8.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  124 EKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEILRKVHSIEYENETLNLENTKLKttlAALKDEVVSVENELSELQ 203
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  204 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItKTKNKNVEKMRGQMESHLKELERVCDSLtaaERRLHEC 283
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-EREIEEERKRRDKLTEEYAELKEELEDL---RAELEEV 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  284 QESLQCCKGKCADQEHTIRELQGQVDgnhnlltklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSN 363
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREIN---------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  364 LKFKEKSAEYTALARQLEAALEEGRQKvAEEIEKMSSRESALQIKILDLETELRKKNEEQ 423
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDL-KEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
167-426 1.46e-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: 44.28  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  167 IEYENETLNLENT--KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 244
Cdd:TIGR02168  673 LERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  245 tktknknvekmrgqmeshLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQvdgnhnlltklsleeen 324
Cdd:TIGR02168  753 ------------------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------------- 797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  325 cliqlkCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESA 404
Cdd:TIGR02168  798 ------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEE 870
                          250       260
                   ....*....|....*....|..
gi 2067662260  405 LQIKILDLETELRKKNEEQNQL 426
Cdd:TIGR02168  871 LESELEALLNERASLEEALALL 892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-388 1.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  82 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 161
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 162 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 241
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 242 NQITKTKNKNVEKmrgqmESHLKELERVCDSLTAAERRLHECQESLQcckgkcADQEHTIRELqgqvdgnhnlltkLSLE 321
Cdd:COG1196   386 EELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELE------EALAELEEEE-------------EEEE 441
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662260 322 EENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 388
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
126-425 1.99e-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: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 126 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 205
Cdd:COG1196   196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 206 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 275
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 276 AERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK-----CENLQQKLEQMDAENKELEK 350
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaEEALLERLERLEEELEELEE 428
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662260 351 KLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQ 425
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK11637 PRK11637
AmiB activator; Provisional
248-421 3.15e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 248 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 317
Cdd:PRK11637   59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 318 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 377
Cdd:PRK11637  139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2067662260 378 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 421
Cdd:PRK11637  217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
180-421 4.19e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 180 KLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitktknknvEKMR 256
Cdd:PRK02224  479 ELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA---------------EELR 543
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 257 GQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEnclIQLKCENLQQ 336
Cdd:PRK02224  544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD---AEDEIERLRE 613
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 337 KLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETEL 416
Cdd:PRK02224  614 KREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690

                  ....*
gi 2067662260 417 RKKNE 421
Cdd:PRK02224  691 EELEE 695
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
62-268 5.22e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  62 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 141
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 142 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 207
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662260 208 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 268
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
88-426 7.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  88 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 161
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 162 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 221
Cdd:PRK03918  283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 222 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 297
Cdd:PRK03918  363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 298 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEEClkhsnLKFKEKSAEYTALA 377
Cdd:PRK03918  442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELE 509
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2067662260 378 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 426
Cdd:PRK03918  510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-273 7.19e-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: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260    1 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 73
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   74 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 150
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  151 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 230
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2067662260  231 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 273
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
35-226 7.88e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  35 QSEKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL---------S 105
Cdd:COG3206   175 KALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLaalraqlgsG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 106 ETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEYENETLNLEN 178
Cdd:COG3206   253 PDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQARE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2067662260 179 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 226
Cdd:COG3206   330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
127-405 1.40e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  127 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 203
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  204 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 279
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  280 LHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKL-----SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLAN 354
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2067662260  355 QEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 405
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
203-435 1.68e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 203 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 280
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 281 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 355
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 356 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 420
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
                         250
                  ....*....|....*
gi 2067662260 421 EEQNQLVCKMNSDPE 435
Cdd:pfam05667 475 ELYKQLVAEYERLPK 489
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
137-250 1.97e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.45  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 137 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 216
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662260 217 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 250
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
263-426 3.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 263 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 342
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 343 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 422
Cdd:COG4717   153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                  ....
gi 2067662260 423 QNQL 426
Cdd:COG4717   229 LEQL 232
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
219-415 3.36e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  219 QVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHECQESLQ 288
Cdd:pfam15921  427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSDLTASLQ 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  289 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 367
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2067662260  368 EKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETE 415
Cdd:pfam15921  587 AMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELE 633
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-237 3.75e-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: 39.65  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260    4 ENLTDNESENTNLKKKVFEKEAHIQELSclfQSEKSLETKIAKWNLQSRMNKNeaivMKEASRQKTVALKKASKVYKQRL 83
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELES----KLDELAEELAELEEKLEELKEEL 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   84 DHFTGAIEKLTSQIRDQEaklsetiSASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILrk 163
Cdd:TIGR02168  354 ESLEAELEELEAELEELE-------SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE-- 424
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662260  164 vhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENL 237
Cdd:TIGR02168  425 ----ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-430 3.88e-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: 39.67  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  197 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 276
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  277 ERRLHECQESLQCCKGKCADQEHTIRELQGQVDgnhnlltKLSlEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQE 356
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLG-EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662260  357 ECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKM 430
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
PTZ00121 PTZ00121
MAEBL; Provisional
57-423 3.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260   57 EAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTELEVQIETMK 136
Cdd:PTZ00121  1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDK 1404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  137 KQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTlie 214
Cdd:PTZ00121  1405 KKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  215 myKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----LHECQESLQ 288
Cdd:PTZ00121  1482 --AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeLKKAEELKK 1559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  289 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQM-DAENKELEKKLANQEECLKHSNLKFK 367
Cdd:PTZ00121  1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLK 1639
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2067662260  368 EKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQ 423
Cdd:PTZ00121  1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEA 1693
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-432 5.72e-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: 39.27  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  248 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVdgnhnlltkLSLEEENCLI 327
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260  328 QLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTalarqleaALEEGRQKVAEEIEKMSSRESALQI 407
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATER 838
                          170       180
                   ....*....|....*....|....*
gi 2067662260  408 KILDLETELRKKNEEQNQLVCKMNS 432
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEE 863
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
330-426 9.01e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662260 330 KCENLQQKLEQMDAENKELEKKLANQEECLKHsnlkfkeksaeytalarqLEAALEEGRQKVAEEIEKmsSRE-SALQIK 408
Cdd:COG2433   414 EIRRLEEQVERLEAEVEELEAELEEKDERIER------------------LERELSEARSEERREIRK--DREiSRLDRE 473
                          90
                  ....*....|....*...
gi 2067662260 409 ILDLETELRKKNEEQNQL 426
Cdd:COG2433   474 IERLERELEEERERIEEL 491
 
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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