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Conserved domains on  [gi|2067662293|ref|NP_001382456|]
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protein BCAP isoform e [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 ...
209-465 1.63e-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: 57.39  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  209 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 288
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  289 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 366
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  367 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 446
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662293  447 KILDLETELRKKNEEQNQL 465
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-312 2.35e-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: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293    4 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 83
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293   84 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 163
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  164 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 240
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662293  241 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 312
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
209-465 1.63e-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: 57.39  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  209 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 288
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  289 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 366
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  367 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 446
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662293  447 KILDLETELRKKNEEQNQL 465
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-465 9.78e-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: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  289 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 356
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  357 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 430
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662293  431 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 465
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-312 2.35e-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: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293    4 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 83
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293   84 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 163
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  164 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 240
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662293  241 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 312
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
56-460 5.25e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  56 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 135
Cdd:PRK02224  333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 136 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 208
Cdd:PRK02224  393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 209 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitk 285
Cdd:PRK02224  473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA--------- 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 286 tknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEncl 365
Cdd:PRK02224  540 ------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD--- 603
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 366 IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQ 445
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQ 680
                         410
                  ....*....|....*
gi 2067662293 446 IKILDLETELRKKNE 460
Cdd:PRK02224  681 AEIGAVENELEELEE 695
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
65-265 2.29e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  65 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 143
Cdd:COG3206   166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 144 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 208
Cdd:COG3206   244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662293 209 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 265
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
258-495 4.01e-04

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: 43.18  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  258 QVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHECQESLQ 327
Cdd:pfam15921  427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSDLTASLQ 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  328 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 406
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  407 EKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQN 485
Cdd:pfam15921  587 AMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
                          250
                   ....*....|
gi 2067662293  486 SLEKSENQNE 495
Cdd:pfam15921  665 SRNELNSLSE 674
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
209-465 1.63e-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: 57.39  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  209 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 288
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  289 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 366
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  367 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 446
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662293  447 KILDLETELRKKNEEQNQL 465
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
162-466 9.01e-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: 51.98  E-value: 9.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  162 IEKTELEVQIETMKKQIINLLEDLKKMEDhgknSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 241
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  242 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHE 321
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAELEELEAELEELESRLEE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  322 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKCENLQQKLEQMDAENKELEKKLANQEECLKHS 401
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662293  402 NLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilDLETELRKKNEEQNQLV 466
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-465 9.78e-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: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  289 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 356
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  357 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 430
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662293  431 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 465
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-312 2.35e-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: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293    4 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 83
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293   84 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 163
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  164 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 240
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662293  241 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 312
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
56-460 5.25e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  56 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 135
Cdd:PRK02224  333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 136 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 208
Cdd:PRK02224  393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 209 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitk 285
Cdd:PRK02224  473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA--------- 539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 286 tknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEncl 365
Cdd:PRK02224  540 ------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD--- 603
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 366 IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQ 445
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQ 680
                         410
                  ....*....|....*
gi 2067662293 446 IKILDLETELRKKNE 460
Cdd:PRK02224  681 AEIGAVENELEELEE 695
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
163-462 8.08e-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: 45.44  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  163 EKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEILRKVHSIEYENETLNLENTKLKttlAALKDEVVSVENELSELQ 242
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  243 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItKTKNKNVEKMRGQMESHLKELERVCDSLtaaERRLHEC 322
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-EREIEEERKRRDKLTEEYAELKEELEDL---RAELEEV 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  323 QESLQCCKGKCADQEHTIRELQGQVDgnhnlltklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSN 402
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREIN---------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  403 LKFKEKSAEYTALARQLEAALEEGRQKvAEEIEKMSSRESALQIKILDLETELRKKNEEQ 462
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDL-KEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
110-395 8.82e-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: 45.43  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  110 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKme 189
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-- 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  190 dhgknsceeilrkvhsIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 269
Cdd:TIGR02168  321 ----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  270 KSRCENLLHKNNQITKTknknVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQVDG 349
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER 458
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2067662293  350 NHNLLTKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANQE 395
Cdd:TIGR02168  459 LEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
121-427 1.63e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 121 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 200
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 201 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 280
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 281 NQITKTKNKNVEKmrgqmESHLKELERVCDSLTAAERRLHECQESLQcckgkcADQEHTIRELqgqvdgnhnlltkLSLE 360
Cdd:COG1196   386 EELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELE------EALAELEEEE-------------EEEE 441
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662293 361 EENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 427
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
165-464 2.11e-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: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 165 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 244
Cdd:COG1196   196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 245 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 314
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 315 AERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK-----CENLQQKLEQMDAENKELEK 389
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaEEALLERLERLEEELEELEE 428
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662293 390 KLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQ 464
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
127-489 2.26e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 127 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 200
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 201 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 260
Cdd:PRK03918  283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 261 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 336
Cdd:PRK03918  363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 337 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEEClkhsnLKFKEKSAEYTALA 416
Cdd:PRK03918  442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELE 509
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662293 417 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 489
Cdd:PRK03918  510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
65-265 2.29e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  65 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 143
Cdd:COG3206   166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 144 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 208
Cdd:COG3206   244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662293 209 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 265
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
258-495 4.01e-04

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: 43.18  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  258 QVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHECQESLQ 327
Cdd:pfam15921  427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSDLTASLQ 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  328 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 406
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  407 EKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQN 485
Cdd:pfam15921  587 AMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
                          250
                   ....*....|
gi 2067662293  486 SLEKSENQNE 495
Cdd:pfam15921  665 SRNELNSLSE 674
PTZ00121 PTZ00121
MAEBL; Provisional
8-505 4.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293    8 DNESENTNLKKKVFEKEAHIQELSCLFQSEKAntlkanRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKiaKWN 87
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEA------RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKA 1317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293   88 LQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTEL 167
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEA 1396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  168 EVQIETMKKQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVE 245
Cdd:PTZ00121  1397 KKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  246 KKQKTliemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----L 319
Cdd:PTZ00121  1477 KKAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeL 1551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  320 HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQM-DAENKELEKKLANQEECL 398
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEE 1631
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  399 KHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEV 478
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
                          490       500
                   ....*....|....*....|....*..
gi 2067662293  479 CLKEVQNSLEKSENQNESIKNYLQFLK 505
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEENKIKAEEAK 1736
PRK11637 PRK11637
AmiB activator; Provisional
287-460 5.41e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.37  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 287 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 356
Cdd:PRK11637   59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 357 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 416
Cdd:PRK11637  139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2067662293 417 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 460
Cdd:PRK11637  217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
297-465 7.15e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 297 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENC-----LIQLKCE 371
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiaRLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 372 NLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDL 451
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170
                  ....*....|....
gi 2067662293 452 ETELRKKNEEQNQL 465
Cdd:COG1196   393 RAAAELAAQLEELE 406
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
101-307 8.26e-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: 41.67  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 101 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 180
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 181 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 246
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662293 247 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 307
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
287-511 1.08e-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: 41.97  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  287 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVdgnhnlltkLSLEEENCLI 366
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  367 QLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTalarqleaALEEGRQKVAEEIEKMSSRESALQI 446
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662293  447 KILDLETELRKKNEEQNQLVCKMNSkaqhQEVCLKEVQNSLEKSENQNESIKNYLQFLKTSYVTM 511
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEE----LEELIEELESELEALLNERASLEEALALLRSELEEL 899
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
302-478 1.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 302 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 381
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 382 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 461
Cdd:COG4717   153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                         170
                  ....*....|....*..
gi 2067662293 462 QNQLVCKMNSKAQHQEV 478
Cdd:COG4717   229 LEQLENELEAAALEERL 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
166-444 1.51e-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: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  166 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 242
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  243 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 318
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  319 LHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKL-----SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLAN 393
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2067662293  394 QEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 444
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
176-289 3.00e-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: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 176 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 255
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662293 256 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 289
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
242-466 3.10e-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: 40.01  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 242 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 319
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 320 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 394
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 395 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 459
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474

                  ....*..
gi 2067662293 460 EEQNQLV 466
Cdd:pfam05667 475 ELYKQLV 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
35-327 3.55e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  35 QSEKAntLKANRFSQSVKVV-HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaivmKEASRQKTVALKK 113
Cdd:COG1196   208 QAEKA--ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 114 ASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSEtisasnawkshyekIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 193
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293 194 NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 273
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2067662293 274 ENLLHKNNQITKTKNKNVEKMRGQMEsHLKELERVCDSLTAAERRLHECQESLQ 327
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
236-469 4.23e-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: 40.05  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  236 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 315
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662293  316 ERRLHECQESLQCCKGKCADQEHTIRELQGQVDgnhnlltKLSlEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQE 395
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLG-EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662293  396 ECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKM 469
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
 
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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