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Conserved domains on  [gi|2067662289|ref|NP_001382449|]
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protein BCAP isoform h [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 ...
301-557 7.31e-09

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: 58.93  E-value: 7.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 380
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  381 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 458
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  459 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 538
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662289  539 KILDLETELRKKNEEQNQL 557
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-587 6.33e-06

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: 49.35  E-value: 6.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   38 CLKQDILNEKT----ELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLK-ISEQKEILIKELDT----FKS 108
Cdd:pfam15921  159 CLKEDMLEDSNtqieQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTeisyLKG 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  109 VKLALEHLLRKrdYKQTGDNLSSMLLENLTDNesentnLKKKVFEKEAHIQELSclfqsEKSLETKIAKWNLQSRMNkne 188
Cdd:pfam15921  239 RIFPVEDQLEA--LKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLT-----EKASSARSQANSIQSQLE--- 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  189 aIVMKEASRQKTValkkaskvYKQRLDHFTGAIEKLTSQIRDQ----EAKLSETISASNAWKSHYEKIVIEKTELEVQIE 264
Cdd:pfam15921  303 -IIQEQARNQNSM--------YMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  265 TMKKQIINLLEDLKKMEdhgknsceeilrKVHSIEYE-NETLNLENTKLKTTLAALKDEvvsvenelselqevekkqktl 343
Cdd:pfam15921  374 NLDDQLQKLLADLHKRE------------KELSLEKEqNKRLWDRDTGNSITIDHLRRE--------------------- 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHE 413
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSD 500
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKH 492
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  493 SNLKFKEKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVC 571
Cdd:pfam15921  581 HGRTAGAMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
                          570
                   ....*....|....*.
gi 2067662289  572 LKEVQNSLEKSENQNE 587
Cdd:pfam15921  659 LNEVKTSRNELNSLSE 674
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-557 7.31e-09

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: 58.93  E-value: 7.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 380
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  381 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 458
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  459 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 538
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662289  539 KILDLETELRKKNEEQNQL 557
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-587 6.33e-06

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: 49.35  E-value: 6.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   38 CLKQDILNEKT----ELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLK-ISEQKEILIKELDT----FKS 108
Cdd:pfam15921  159 CLKEDMLEDSNtqieQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTeisyLKG 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  109 VKLALEHLLRKrdYKQTGDNLSSMLLENLTDNesentnLKKKVFEKEAHIQELSclfqsEKSLETKIAKWNLQSRMNkne 188
Cdd:pfam15921  239 RIFPVEDQLEA--LKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLT-----EKASSARSQANSIQSQLE--- 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  189 aIVMKEASRQKTValkkaskvYKQRLDHFTGAIEKLTSQIRDQ----EAKLSETISASNAWKSHYEKIVIEKTELEVQIE 264
Cdd:pfam15921  303 -IIQEQARNQNSM--------YMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  265 TMKKQIINLLEDLKKMEdhgknsceeilrKVHSIEYE-NETLNLENTKLKTTLAALKDEvvsvenelselqevekkqktl 343
Cdd:pfam15921  374 NLDDQLQKLLADLHKRE------------KELSLEKEqNKRLWDRDTGNSITIDHLRRE--------------------- 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHE 413
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSD 500
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKH 492
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  493 SNLKFKEKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVC 571
Cdd:pfam15921  581 HGRTAGAMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
                          570
                   ....*....|....*.
gi 2067662289  572 LKEVQNSLEKSENQNE 587
Cdd:pfam15921  659 LNEVKTSRNELNSLSE 674
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
381-557 7.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  381 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 448
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  449 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 522
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662289  523 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 557
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-524 4.75e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918  360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918  440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaeiVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918  520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE----LEEELAELLKELEELGFESVE 588
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 382 NVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGnhnlLTKLSLEEENCLI 458
Cdd:PRK03918  589 ELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE----LEKKYSEEEYEEL 664
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAALEEGRQKVAE 524
Cdd:PRK03918  665 REEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKK 732
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-581 8.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 219 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 292
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 352
Cdd:PRK03918  283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 353 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 428
Cdd:PRK03918  363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 429 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALA 508
Cdd:PRK03918  442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE 509
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662289 509 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 581
Cdd:PRK03918  510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-399 2.47e-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: 43.60  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 193 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 272
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 273 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 338
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662289 339 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 399
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-404 5.58e-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: 43.12  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  132 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 204
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  205 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 281
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  282 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2067662289  362 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 404
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
268-381 1.40e-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: 39.61  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 268 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 347
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662289 348 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 381
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-557 7.31e-09

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: 58.93  E-value: 7.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 380
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  381 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 458
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  459 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 538
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
                          250
                   ....*....|....*....
gi 2067662289  539 KILDLETELRKKNEEQNQL 557
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-558 3.79e-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: 53.52  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  254 IEKTELEVQIETMKKQIINLLEDLKKMEDhgknSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 333
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHE 413
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAELEELEAELEELESRLEE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKCENLQQKLEQMDAENKELEKKLANQEECLKHS 493
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289  494 NLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilDLETELRKKNEEQNQLV 558
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-529 4.52e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  194 EASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSET-------ISASNAWKSHYEKIVIEKTELEVQIETM 266
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarlEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  267 KKQIINLLEDLKKMEDHGKNSCEEIlrkvhsieyenETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEM 346
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI-----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  347 YKTQVQKLQEAAEIVKSRCENLlhknnqitktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCA 426
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESL-----------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  427 DQEHTIRELQGQVDGNHNLLTKLSLEEENclIQLKCENLQQKL---EQMDAEN-KELEKKLANQEECLKHS--------- 493
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEG--LEVRIDNLQERLseeYSLTLEEaEALENKIEDDEEEARRRlkrlenkik 982
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2067662289  494 -----NL----KFKEKSAEYTALARQLEaALEEGRQKVAEEIEKM 529
Cdd:TIGR02168  983 elgpvNLaaieEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEI 1026
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
38-587 6.33e-06

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: 49.35  E-value: 6.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   38 CLKQDILNEKT----ELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLK-ISEQKEILIKELDT----FKS 108
Cdd:pfam15921  159 CLKEDMLEDSNtqieQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTeisyLKG 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  109 VKLALEHLLRKrdYKQTGDNLSSMLLENLTDNesentnLKKKVFEKEAHIQELSclfqsEKSLETKIAKWNLQSRMNkne 188
Cdd:pfam15921  239 RIFPVEDQLEA--LKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLT-----EKASSARSQANSIQSQLE--- 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  189 aIVMKEASRQKTValkkaskvYKQRLDHFTGAIEKLTSQIRDQ----EAKLSETISASNAWKSHYEKIVIEKTELEVQIE 264
Cdd:pfam15921  303 -IIQEQARNQNSM--------YMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  265 TMKKQIINLLEDLKKMEdhgknsceeilrKVHSIEYE-NETLNLENTKLKTTLAALKDEvvsvenelselqevekkqktl 343
Cdd:pfam15921  374 NLDDQLQKLLADLHKRE------------KELSLEKEqNKRLWDRDTGNSITIDHLRRE--------------------- 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHE 413
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSD 500
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKH 492
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  493 SNLKFKEKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVC 571
Cdd:pfam15921  581 HGRTAGAMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
                          570
                   ....*....|....*.
gi 2067662289  572 LKEVQNSLEKSENQNE 587
Cdd:pfam15921  659 LNEVKTSRNELNSLSE 674
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
381-557 7.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  381 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 448
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  449 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 522
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2067662289  523 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 557
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-487 4.42e-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: 46.59  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  202 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKme 281
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-- 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  282 dhgknsceeilrkvhsIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168  321 ----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  362 KSRCENLLHKNNQITKTknknVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQVDG 441
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER 458
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2067662289  442 NHNLLTKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANQE 487
Cdd:TIGR02168  459 LEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-524 4.75e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918  360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918  440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaeiVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918  520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE----LEEELAELLKELEELGFESVE 588
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 382 NVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGnhnlLTKLSLEEENCLI 458
Cdd:PRK03918  589 ELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE----LEKKYSEEEYEEL 664
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAALEEGRQKVAE 524
Cdd:PRK03918  665 REEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKK 732
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-581 8.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 219 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 292
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 352
Cdd:PRK03918  283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 353 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 428
Cdd:PRK03918  363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 429 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALA 508
Cdd:PRK03918  442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE 509
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662289 509 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 581
Cdd:PRK03918  510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-585 8.87e-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: 45.88  E-value: 8.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289    2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  162 SCLFQSEKSLETKIAKWNLQSRMNKNEAIvmkEASRQKTVALKKASKVYKQRLDHFTG---AIEKLTSQIRDQEAKLSE- 237
Cdd:pfam15921  432 EALLKAMKSECQGQMERQMAAIQGKNESL---EKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASLQEk 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  238 --TISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLK--KMEDHGKNSCEEILRKvhSIEYENETLNLENTK-- 311
Cdd:pfam15921  509 erAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEalKLQMAEKDKVIEILRQ--QIENMTQLVGQHGRTag 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  312 -LKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQ-EAAEIVKSRCENLlhknnQITKTKNKNVEKMRGQ 389
Cdd:pfam15921  587 aMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGSERL-----RAVKDIKQERDQLLNE 661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  390 MESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKL 469
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQI 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  470 EQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 549
Cdd:pfam15921  737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 2067662289  550 KNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 585
Cdd:pfam15921  816 ASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-519 9.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 9.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 292
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 372
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 373 NQITKTKNKNVEKmrgqmESHLKELERVCDSLTAAERRLHECQESLQcckgkcADQEHTIRELqgqvdgnhnlltkLSLE 452
Cdd:COG1196   386 EELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELE------EALAELEEEE-------------EEEE 441
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662289 453 EENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 519
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
257-556 1.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 257 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 336
Cdd:COG1196   196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 337 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 406
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 407 AERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK-----CENLQQKLEQMDAENKELEK 481
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaEEALLERLERLEEELEELEE 428
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289 482 KLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQ 556
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK11637 PRK11637
AmiB activator; Provisional
379-552 1.58e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 379 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 448
Cdd:PRK11637   59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 449 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 508
Cdd:PRK11637  139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2067662289 509 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 552
Cdd:PRK11637  217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
197-552 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 197 RQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLED 276
Cdd:PRK02224  362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 277 LKKME---DHGK-NSCEEILRK---VHSIEYENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEM 346
Cdd:PRK02224  442 VEEAEallEAGKcPECGQPVEGsphVETIEEDRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEER 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 347 YKTQVQKLQEAAEIVKSRCENLlhknnqitktknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCA 426
Cdd:PRK02224  518 REDLEELIAERRETIEEKRERA---------------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 427 DQEHTIRELQgqvdgnhNLLTKLSLEEEnclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYta 506
Cdd:PRK02224  583 ELKERIESLE-------RIRTLLAAIAD---AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE-- 650
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2067662289 507 lARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNE 552
Cdd:PRK02224  651 -AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-399 2.47e-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: 43.60  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 193 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 272
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 273 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 338
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662289 339 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 399
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
389-557 5.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 389 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENC-----LIQLKCE 463
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiaRLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 464 NLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDL 543
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                         170
                  ....*....|....
gi 2067662289 544 ETELRKKNEEQNQL 557
Cdd:COG1196   393 RAAAELAAQLEELE 406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-404 5.58e-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: 43.12  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  132 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 204
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  205 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 281
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  282 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2067662289  362 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 404
Cdd:TIGR02168  942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
379-603 5.92e-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: 43.12  E-value: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  379 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVdgnhnlltkLSLEEENCLI 458
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  459 QLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTalarqleaALEEGRQKVAEEIEKMSSRESALQI 538
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289  539 KILDLETELRKKNEEQNQLVCKMNSkaqhQEVCLKEVQNSLEKSENQNESIKNYLQFLKTSYVTM 603
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEE----LEELIEELESELEALLNERASLEEALALLRSELEEL 899
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
394-570 7.34e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 394 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 473
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 474 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 553
Cdd:COG4717   153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                         170
                  ....*....|....*..
gi 2067662289 554 QNQLVCKMNSKAQHQEV 570
Cdd:COG4717   229 LEQLENELEAAALEERL 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
258-536 7.39e-04

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: 42.75  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  258 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  335 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 410
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  411 LHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKL-----SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLAN 485
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2067662289  486 QEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 536
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-357 9.20e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 166 QSEKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL---------S 236
Cdd:COG3206   175 KALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLaalraqlgsG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 237 ETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEYENETLNLEN 309
Cdd:COG3206   253 PDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQARE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2067662289 310 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 357
Cdd:COG3206   330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
PTZ00121 PTZ00121
MAEBL; Provisional
188-597 1.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  188 EAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTELEVQIETMK 267
Cdd:PTZ00121  1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDK 1404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  268 KQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTlie 345
Cdd:PTZ00121  1405 KKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  346 myKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----LHECQESLQ 419
Cdd:PTZ00121  1482 --AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeLKKAEELKK 1559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  420 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQM-DAENKELEKKLANQEECLKHSNLKFK 498
Cdd:PTZ00121  1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLK 1639
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  499 EKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNS 578
Cdd:PTZ00121  1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
                          410
                   ....*....|....*....
gi 2067662289  579 LEKSENQNESIKNYLQFLK 597
Cdd:PTZ00121  1718 AEELKKAEEENKIKAEEAK 1736
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
268-381 1.40e-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: 39.61  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 268 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 347
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662289 348 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 381
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
95-368 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   95 QKEILIKELDTFKSVKLALEHLLRKrdykqtGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCLfQSEKSLETK 174
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  175 IAKWNLQSRMNKNEAI-VMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIV 253
Cdd:TIGR02168  306 ILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  254 IEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 333
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE------ELLKKLEEAELKELQAELEELEEELEELQEELERL 459
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2067662289  334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENL 368
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSL 494
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
334-558 1.66e-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: 41.55  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 411
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 412 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 486
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 487 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 551
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474

                  ....*..
gi 2067662289 552 EEQNQLV 558
Cdd:pfam05667 475 ELYKQLV 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
328-561 2.20e-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: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  328 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 407
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  408 ERRLHECQESLQCCKGKCADQEHTIRELQGQVDgnhnlltKLSlEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQE 487
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLG-EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662289  488 ECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKM 561
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
305-594 3.91e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  305 LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhkNNQITKTKNkNVE 384
Cdd:TIGR00606  693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV---NRDIQRLKN-DIE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  385 KMRGQMESHLKELERVCDSLTAAERrLHECQESLQcckgkcaDQEHTIRELQGQVDGNHNLLTKLSLEEENcliqlkcEN 464
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVTI-MERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEK-------QE 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  465 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLE--AALEEGRQKVAEEIEKMSSRESALQIKILD 542
Cdd:TIGR00606  834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrrQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2067662289  543 LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNSLEKSENQNESIKNYLQ 594
Cdd:TIGR00606  914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-368 6.08e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289   43 ILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKrdY 122
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--L 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  123 KQTGDNLSSMLLENLTDN-ESENTNLKKKVFEKEAHIQELSCLFQSeKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTV 201
Cdd:TIGR02169  778 EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  202 ALKKAskvykqRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 281
Cdd:TIGR02169  857 ENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  282 DHGKnsceEILRKVHSIEYE-NETLNLEntKLKTTLAALKDEVVSVEN-ELSELQEVEKKQKTLIEmYKTQVQKLQEAAE 359
Cdd:TIGR02169  931 EELS----EIEDPKGEDEEIpEEELSLE--DVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDE-LKEKRAKLEEERK 1003

                   ....*....
gi 2067662289  360 IVKSRCENL 368
Cdd:TIGR02169 1004 AILERIEEY 1012
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
127-587 6.27e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.82  E-value: 6.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  127 DNLSSMLLENLTDNESENTNLKKK---------------VFEKEAHiqELSCLFQSEKSLETKIAKWNLQSRMNKNEaiV 191
Cdd:pfam12128  196 RDVKSMIVAILEDDGVVPPKSRLNrqqvehwirdiqaiaGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSD--E 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  192 MKEASRQKtvALKKASKVYKQRLDHFTG----AIEKLTSQIRDQEAKLS---ETISASNAWKSHYEKIVIEKTELEV-QI 263
Cdd:pfam12128  272 TLIASRQE--ERQETSAELNQLLRTLDDqwkeKRDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIETAAADQeQL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  264 ETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETlnlENTKLKTTLAALKDEVVSVENELSElqEVEKKQKTL 343
Cdd:pfam12128  350 PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVAED--DLQALESEL 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKT---------KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHEC 414
Cdd:pfam12128  425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllqlenFDERIERAREEQEAANAEVERLQSELRQARKRRDQA 504
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  415 QESLQCCKGKCADQEHTIRELQGQVD-GNHNLLTKLSLE---------------------------EENCLIQLKCENLQ 466
Cdd:pfam12128  505 SEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEapdweqsigkvispellhrtdldpevwDGSVGGELNLYGVK 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289  467 QKLEQMD-----AENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAA-LEEGRQKVA-----EEIEKMSSRESA 535
Cdd:pfam12128  585 LDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAsREETFARTAlknarLDLRRLFDEKQS 664
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2067662289  536 LQIKILD-LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNslEKSENQNE 587
Cdd:pfam12128  665 EKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTE 715
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
461-557 9.41e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 461 KCENLQQKLEQMDAENKELEKKLANQEECLKHsnlkfkeksaeytalarqLEAALEEGRQKVAEEIEKmsSRE-SALQIK 539
Cdd:COG2433   414 EIRRLEEQVERLEAEVEELEAELEEKDERIER------------------LERELSEARSEERREIRK--DREiSRLDRE 473
                          90
                  ....*....|....*...
gi 2067662289 540 ILDLETELRKKNEEQNQL 557
Cdd:COG2433   474 IERLERELEEERERIEEL 491
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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