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Conserved domains on  [gi|296179397|ref|NP_001007023|]
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protein BCAP isoform b [Homo sapiens]

Protein Classification

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 ...
377-625 1.73e-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: 57.77  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   377 ISSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKNKNVEKMRG 456
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   457 QMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLIQLKCENLQ 534
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEIQELQ 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   535 QKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILDLETE 614
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQ 911
                          250
                   ....*....|.
gi 296179397   615 LRKKNEEQNQL 625
Cdd:TIGR02169  912 IEKKRKRLSEL 922
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-617 1.31e-05

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397    33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSE--KANTlKANRFSQSVK 183
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSEltEART-ERDQFSQESG 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   184 VVHERLQ---IQIHKREAENDKLKEYVKSLetkiakWNlqsrMNKNEAIVMKEASRQ---KTVALKKASKVYKQRLDHFT 257
Cdd:pfam15921  374 NLDDQLQkllADLHKREKELSLEKEQNKRL------WD----RDTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECQ 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYE---KIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILR-- 332
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlr 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   333 -----KVHSIEY-ENETLNLENTK-----LKLRFPcriTESKNMNIL--IVLDMLCYISSEKTTLAALKDEVVSVENELS 399
Cdd:pfam15921  524 srvdlKLQELQHlKNEGDHLRNVQteceaLKLQMA---EKDKVIEILrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   400 ELQEVEKKQKTLIEMYKTQVQKLQEAA---EIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAE 476
Cdd:pfam15921  601 DRRLELQEFKILKDKKDAKIRELEARVsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   477 RRLHECQESLQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 556
Cdd:pfam15921  681 RNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179397   557 CLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 617
Cdd:pfam15921  756 AMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
377-625 1.73e-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: 57.77  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   377 ISSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKNKNVEKMRG 456
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   457 QMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLIQLKCENLQ 534
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEIQELQ 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   535 QKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILDLETE 614
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQ 911
                          250
                   ....*....|.
gi 296179397   615 LRKKNEEQNQL 625
Cdd:TIGR02169  912 IEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
449-625 6.65e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  449 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 516
Cdd:COG4913   242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  517 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 590
Cdd:COG4913   321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 296179397  591 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 625
Cdd:COG4913   401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-617 1.31e-05

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: 48.58  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397    33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSE--KANTlKANRFSQSVK 183
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSEltEART-ERDQFSQESG 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   184 VVHERLQ---IQIHKREAENDKLKEYVKSLetkiakWNlqsrMNKNEAIVMKEASRQ---KTVALKKASKVYKQRLDHFT 257
Cdd:pfam15921  374 NLDDQLQkllADLHKREKELSLEKEQNKRL------WD----RDTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECQ 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYE---KIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILR-- 332
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlr 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   333 -----KVHSIEY-ENETLNLENTK-----LKLRFPcriTESKNMNIL--IVLDMLCYISSEKTTLAALKDEVVSVENELS 399
Cdd:pfam15921  524 srvdlKLQELQHlKNEGDHLRNVQteceaLKLQMA---EKDKVIEILrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   400 ELQEVEKKQKTLIEMYKTQVQKLQEAA---EIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAE 476
Cdd:pfam15921  601 DRRLELQEFKILKDKKDAKIRELEARVsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   477 RRLHECQESLQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 556
Cdd:pfam15921  681 RNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179397   557 CLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 617
Cdd:pfam15921  756 AMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-625 4.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSI 337
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 338 EYENETLNLENTKLKLRFPCRITESKNMNILIVLDMLcyiSSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKT 417
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 418 QVQKLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKC 493
Cdd:PRK03918 360 RHELYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 494 ADQEHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEEClkhsnLKFKEKSAEYT 573
Cdd:PRK03918 439 PVCGRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLK 506
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 296179397 574 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 625
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
402-634 7.30e-04

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: 42.71  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  402 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRL-- 479
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPtk 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  480 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 554
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  555 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 619
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
                         250
                  ....*....|....*
gi 296179397  620 EEQNQLVCKMNSDPE 634
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 ...
377-625 1.73e-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: 57.77  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   377 ISSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKNKNVEKMRG 456
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   457 QMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLIQLKCENLQ 534
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEIQELQ 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   535 QKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILDLETE 614
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQ 911
                          250
                   ....*....|.
gi 296179397   615 LRKKNEEQNQL 625
Cdd:TIGR02169  912 IEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
449-625 6.65e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  449 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 516
Cdd:COG4913   242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  517 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 590
Cdd:COG4913   321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 296179397  591 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 625
Cdd:COG4913   401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
33-617 1.31e-05

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: 48.58  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397    33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSE--KANTlKANRFSQSVK 183
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSEltEART-ERDQFSQESG 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   184 VVHERLQ---IQIHKREAENDKLKEYVKSLetkiakWNlqsrMNKNEAIVMKEASRQ---KTVALKKASKVYKQRLDHFT 257
Cdd:pfam15921  374 NLDDQLQkllADLHKREKELSLEKEQNKRL------WD----RDTGNSITIDHLRRElddRNMEVQRLEALLKAMKSECQ 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYE---KIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILR-- 332
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlr 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   333 -----KVHSIEY-ENETLNLENTK-----LKLRFPcriTESKNMNIL--IVLDMLCYISSEKTTLAALKDEVVSVENELS 399
Cdd:pfam15921  524 srvdlKLQELQHlKNEGDHLRNVQteceaLKLQMA---EKDKVIEILrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   400 ELQEVEKKQKTLIEMYKTQVQKLQEAA---EIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAE 476
Cdd:pfam15921  601 DRRLELQEFKILKDKKDAKIRELEARVsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   477 RRLHECQESLQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 556
Cdd:pfam15921  681 RNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179397   557 CLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 617
Cdd:pfam15921  756 AMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
463-625 2.39e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 463 KELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDA 542
Cdd:COG1196  267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEE 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 543 ENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmSSRESALQIKILDLETELRKKNEEQ 622
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEEL 423

                 ...
gi 296179397 623 NQL 625
Cdd:COG1196  424 EEL 426
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-625 4.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSI 337
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 338 EYENETLNLENTKLKLRFPCRITESKNMNILIVLDMLcyiSSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKT 417
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 418 QVQKLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKC 493
Cdd:PRK03918 360 RHELYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 494 ADQEHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEEClkhsnLKFKEKSAEYT 573
Cdd:PRK03918 439 PVCGRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLK 506
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 296179397 574 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 625
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
PRK11637 PRK11637
AmiB activator; Provisional
447-620 7.78e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 447 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 516
Cdd:PRK11637  59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 517 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 576
Cdd:PRK11637 139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296179397 577 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 620
Cdd:PRK11637 217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
384-626 1.19e-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: 45.43  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   384 LAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSrceNLLHKNNQITKTKNKNVEK---------- 453
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER---QLEELEAQLEELESKLDELaeelaeleek 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   454 ---MRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKC 530
Cdd:TIGR02168  346 leeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQ 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   531 ENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilD 610
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----R 496
                          250
                   ....*....|....*.
gi 296179397   611 LETELRKKNEEQNQLV 626
Cdd:TIGR02168  497 LQENLEGFSEGVKALL 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
384-625 2.87e-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: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   384 LAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktknknvekmrgqmeshLK 463
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------------------SK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   464 ELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQvdgnhnlltklsleeencliqlkCENLQQKLEQMDAE 543
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-----------------------LKALREALDELRAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   544 NKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQN 623
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNERASLEEALA 890

                   ..
gi 296179397   624 QL 625
Cdd:TIGR02168  891 LL 892
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
384-620 6.12e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 384 LAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitktknknvEKMRGQMES 460
Cdd:PRK02224 484 LEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA---------------EELRERAAE 548
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 461 HLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEnclIQLKCENLQQKLEQM 540
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD---AEDEIERLREKREAL 618
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 541 DAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNE 620
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
402-634 7.30e-04

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: 42.71  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  402 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRL-- 479
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPtk 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  480 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 554
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397  555 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 619
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
                         250
                  ....*....|....*
gi 296179397  620 EEQNQLVCKMNSDPE 634
Cdd:pfam05667 475 ELYKQLVAEYERLPK 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
241-518 9.07e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 9.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   241 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 320
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   321 ---DHGKNSCEEILRKVHSIEYENETLNLENTKLKLRFPCRITESKNMnilivldmlcyisseKTTLAALKDEVVSVENE 397
Cdd:TIGR02168  323 aqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL---------------ESRLEELEEQLETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   398 LSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLhknnqiTKTKNKNVEKMRGQMESHLKELERVCDSLTAAER 477
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL------KKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 296179397   478 RLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLS 518
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-567 1.24e-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: 42.03  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397     2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397    82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   162 SCLFQSEKANtlkanrfsqsvkvVHERLQIQIHKREAENDKLkEYVKSLETKI--AKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:pfam15921  432 EALLKAMKSE-------------CQGQMERQMAAIQGKNESL-EKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERT 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   240 VALKKASKVYKQRLDHFTGA-IEKLTSQIrdqEAKLSETISASNAW------KSHYEKIVIEKTELEVQIETMKKQIINL 312
Cdd:pfam15921  498 VSDLTASLQEKERAIEATNAeITKLRSRV---DLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQIENM 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   313 LEDLKKmedHGKNSCEEILRKVHsIEYENETLNLENTKLKLrfpcrITESKNMNILIVLDMLCYISSEKTTLAALKDEvv 392
Cdd:pfam15921  575 TQLVGQ---HGRTAGAMQVEKAQ-LEKEINDRRLELQEFKI-----LKDKKDAKIRELEARVSDLELEKVKLVNAGSE-- 643
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   393 svenELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKnvekMRGQMESHLKELERVCDSL 472
Cdd:pfam15921  644 ----RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK----LKMQLKSAQSELEQTRNTL 715
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397   473 TAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLT------------KLSLEEENCLIQLKCENLQQKLEQM 540
Cdd:pfam15921  716 KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTnankekhflkeeKNKLSQELSTVATEKNKMAGELEVL 795
                          570       580
                   ....*....|....*....|....*..
gi 296179397   541 DAENKELEKKLANQEECLKHSNLKFKE 567
Cdd:pfam15921  796 RSQERRLKEKVANMEVALDKASLQFAE 822
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
462-625 1.41e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 462 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 541
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179397 542 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 621
Cdd:COG4717  153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                 ....
gi 296179397 622 QNQL 625
Cdd:COG4717  229 LEQL 232
 
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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