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Conserved domains on  [gi|1958789722|ref|XP_038935189|]
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caspase recruitment domain-containing protein 10 isoform X5 [Rattus norvegicus]

Protein Classification

CARD_CARD10_CARMA3 and Smc domain-containing protein( domain architecture ID 12962293)

CARD_CARD10_CARMA3 and Smc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 76-161 3.30e-53

Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260069  Cd Length: 86  Bit Score: 177.03  E-value: 3.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08807    81 HFTLLT 86
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-499 2.26e-13

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789722 428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
 
Name Accession Description Interval E-value
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 76-161 3.30e-53

Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260069  Cd Length: 86  Bit Score: 177.03  E-value: 3.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08807    81 HFTLLT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 77-163 2.55e-15

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 71.44  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  77 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:pfam00619   1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 1958789722 156 HFTLLTGQ 163
Cdd:pfam00619  78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-499 2.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789722 428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-499 4.23e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.15  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  193 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 272
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  273 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 352
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  353 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 432
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789722  433 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
mukB PRK04863
chromosome partition protein MukB;
204-484 6.88e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  204 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdweagSLELLRLKDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 281
Cdd:PRK04863   844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR-----LLPRLNLLADETLAD-RVEEIREQLDEAEEAKRFVQQh 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  282 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 350
Cdd:PRK04863   917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  351 PGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 430
Cdd:PRK04863   997 AEQERTR------AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958789722  431 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
Cdd:PRK04863  1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 186-493 2.31e-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: 41.26  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  186 MTEVRRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRlaql 265
Cdd:pfam15921  333 LREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR---- 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  266 sEEKNSAVLRSrdLQLAVDQLKLKVSRLEeecALLRRGRGPPPGaeEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQ 345
Cdd:pfam15921  407 -DTGNSITIDH--LRRELDDRNMEVQRLE---ALLKAMKSECQG--QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  346 QEMSRPGAagsERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH---RTLLKDCDLYKH 422
Cdd:pfam15921  479 KVVEELTA---KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKL 555

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789722  423 RMA-------TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQ 493
Cdd:pfam15921  556 QMAekdkvieILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
 
Name Accession Description Interval E-value
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 76-161 3.30e-53

Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260069  Cd Length: 86  Bit Score: 177.03  E-value: 3.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08807    81 HFTLLT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
 76-161 2.40e-39

Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260055  Cd Length: 84  Bit Score: 139.43  E-value: 2.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPcrANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08785     1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08785    79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
 76-161 9.49e-36

Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD11, also known as caspase recruitment domain-containing membrane-associated guanylate kinase protein 1 (CARMA1). CARMA1, together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), form the L-CBM signalosome (CBM complex in lymphoid immune cells) which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARMA1 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260070  Cd Length: 86  Bit Score: 129.36  E-value: 9.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08808     1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08808    81 LYKLVT 86
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 77-161 3.26e-24

Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260071  Cd Length: 86  Bit Score: 96.91  E-value: 3.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  77 WERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 156
Cdd:cd08809     2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81


                  ....*
gi 1958789722 157 FTLLT 161
Cdd:cd08809    82 YKKIT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
 76-161 4.00e-24

Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260068  Cd Length: 86  Bit Score: 96.48  E-value: 4.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08806     1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80


                  ....*.
gi 1958789722 156 HFTLLT 161
Cdd:cd08806    81 LYTQVT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 77-163 2.55e-15

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 71.44  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  77 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:pfam00619   1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 1958789722 156 HFTLLTGQ 163
Cdd:pfam00619  78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-499 2.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789722 428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 84-156 1.59e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 60.22  E-value: 1.59e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789722  84 RHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 156
Cdd:cd01671     5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE---KTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPH 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-499 4.23e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.15  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  193 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 272
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  273 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 352
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  353 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 432
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789722  433 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-498 7.74e-10

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: 62.39  E-value: 7.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  197 KSQLHREQQLQARGRALEEERAGLEQRLREQQ-----------AAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQL 265
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIEnrldelsqelsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  266 SEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPppgaeekEKEPDGVDLLSELRAENQRLTASLQELQEGLQ 345
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  346 QEMSRPGAAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMA 425
Cdd:TIGR02169  823 RLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789722  426 TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLttvtSLEGTKAMLEAQLQRTQ 498
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL----SLEDVQAELQRVEEEIR 968
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 78-150 5.21e-09

Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260072 [Multi-domain]  Cd Length: 85  Bit Score: 53.50  E-value: 5.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789722  78 ERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALE 150
Cdd:cd08810     3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR---TTRKKRVDKLLDILAREGPDGLDALIESIR 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-484 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 190 RRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 269
Cdd:COG1196   262 LAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 270 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaeekekepdgVDLLSELRAENQRLTASLQELQEGLQQEMS 349
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---------------AEAEEELEELAEELLEALRAAAELAAQLEE 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 350 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 429
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958789722 430 QLEEiEKERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDELLTTVTSLE 484
Cdd:COG1196   485 ELAE-AAARLLLLLEAEADYEGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYE 537
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 222-498 2.52e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 222 QRLREQQAAQERCQRLREDWEAGSLELLRLKDENymIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallr 301
Cdd:COG1196   203 EPLERQAEKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLE----- 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 302 rgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWRE----AQDSRQE 377
Cdd:COG1196   276 --------LEELELE------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEELEE 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 378 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLI 457
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958789722 458 EKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 191-499 3.56e-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: 50.44  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  191 RLREARKsQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELL-----RLKDENYMIAMRLAQL 265
Cdd:TIGR02168  173 RRKETER-KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  266 SEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 345
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEE-------------IEELQKE------LYALANEISRLEQQKQILRERLA 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  346 QeMSRPGAAGSERIL-----LDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLY 420
Cdd:TIGR02168  313 N-LERQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789722  421 KHRMATVLAQLEEIEKERDQAIQSRDRiqLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-486 3.81e-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: 50.44  E-value: 3.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  187 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRL-----------REQQAAQERCQRLREDWEAGSLELLRLKDEN 255
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeeelaeaeAEIEELEAQIEQLKEELKALREALDELRAEL 812

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  256 YMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGppPGAEEKEKEPDGVDLLSELRAENQRLTA 335
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--ELEELIEELESELEALLNERASLEEALA 890

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  336 SLQELQEGLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDkYLQEMedLRLKHRTLLK 415
Cdd:TIGR02168  891 LLRSELEELSEE-------------LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQER--LSEEYSLTLE 954

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789722  416 DcdlykhrmatVLAQLEEIEKERDQAIQSRDRIQLQYSQ-------SLIEKDQYRKQVRGLEAERDELLTTVTSLEGT 486
Cdd:TIGR02168  955 E----------AEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-350 2.06e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  190 RRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQERCQRLRE------DWEAGSLELLRLKDE-------NY 256
Cdd:COG4913    609 RAKLAALEAEL---AELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAElerldasSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  257 MIA---MRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAEN--Q 331
Cdd:COG4913    686 DLAaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAveR 765

                          170
                   ....*....|....*....
gi 1958789722  332 RLTASLQELQEGLQQEMSR 350
Cdd:COG4913    766 ELRENLEERIDALRARLNR 784
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 187-476 2.31e-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: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 187 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEA-----------GSLELLRLKDEN 255
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalllaglrglaGAVAVLIGVEAA 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 256 YMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLK-LKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAENQRLT 334
Cdd:COG1196   536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 335 ASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQD-----------SRQELCQKLHAVQGELQWAEELRDKYLQEM 403
Cdd:COG1196   616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggSRRELLAALLEAEAELEELAERLAEEELEL 695

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 404 EDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEK-----------DQYRKQVRGLEAE 472
Cdd:COG1196   696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELERLERE 775


                  ....
gi 1958789722 473 RDEL 476
Cdd:COG1196   776 IEAL 779
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 189-454 2.72e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  189 VRRLREARK----SQLH------REQQLQARGRALEEERAGLEQRLREQQAAQERCQRL------------RED-WEAGS 245
Cdd:COG3096    419 VQALEKARAlcglPDLTpenaedYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQaWQTAR 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  246 lELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKlkvsrleeecALLRRGRGPPPGAEEKEkepdgvDLLSE 325
Cdd:COG3096    499 -ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----------EFCQRIGQQLDAAEELE------ELLAE 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  326 LRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQklhavqgelQWAEELRDkyLQEMED 405
Cdd:COG3096    562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE---------QSGEALAD--SQEVTA 630

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958789722  406 LrlkhrtllkdcdlykhrMATVLAQLEEIEKERDQAIQSRDRIQLQYSQ 454
Cdd:COG3096    631 A-----------------MQQLLEREREATVERDELAARKQALESQIER 662
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 211-484 4.39e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  211 RALEEERAGLEQRLrEQQAAQERCQRLREDWEAGSLELLR--------LKDENymIAMRLAQLSEEKNSAvlrsRDLQLA 282
Cdd:COG3096    839 AALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADET--LADRLEELREELDAA----QEAQAF 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  283 VDQLKLKVSRLEEECALLRRgrgpPPGAEEkekepdgvdllsELRAENQRLTASLQELQEG---LQQEMSR--------- 350
Cdd:COG3096    912 IQQHGKALAQLEPLVAVLQS----DPEQFE------------QLQADYLQAKEQQRRLKQQifaLSEVVQRrphfsyeda 975

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  351 PGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELqwaeelrDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQ 430
Cdd:COG3096    976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLASLKSSRDAKQQTLQELEQELEELGVQ 1048

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958789722  431 LEEIEKERdqAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
Cdd:COG3096   1049 ADAEAEER--ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
mukB PRK04863
chromosome partition protein MukB;
204-484 6.88e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  204 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdweagSLELLRLKDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 281
Cdd:PRK04863   844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR-----LLPRLNLLADETLAD-RVEEIREQLDEAEEAKRFVQQh 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  282 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 350
Cdd:PRK04863   917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  351 PGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 430
Cdd:PRK04863   997 AEQERTR------AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958789722  431 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
Cdd:PRK04863  1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
mukB PRK04863
chromosome partition protein MukB;
192-294 8.44e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 8.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  192 LREARkSQLHREQQLQARGRALEEeragLEQRLREQQAAQER----CQRLREDWEAGS-LELLRLKDEnymiaMRLAQLS 266
Cdd:PRK04863   502 LRRLR-EQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLlaefCKRLGKNLDDEDeLEQLQEELE-----ARLESLS 571

                           90       100
                   ....*....|....*....|....*...
gi 1958789722  267 EEKNSAVLRSRDLQLAVDQLKLKVSRLE 294
Cdd:PRK04863   572 ESVSEARERRMALRQQLEQLQARIQRLA 599
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 211-496 1.01e-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: 45.83  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  211 RALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDenymiamRLAQLSEEKNSAvLRSRDLQLAVDQLKLKV 290
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRREREKA-ERYQALLKEKREYEGYE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  291 SRLEEEcallrrgrgpppgAEEKEKEpdgvdllsELRAENQRLTASLQELQEGLQQEMSRPGAAgsERILLDILEHDWRE 370
Cdd:TIGR02169  228 LLKEKE-------------ALERQKE--------AIERQLASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDL 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  371 AQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQ---AIQSRD- 446
Cdd:TIGR02169  285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKe 364

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  447 -----RIQLQ-----YSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 496
Cdd:TIGR02169  365 eledlRAELEevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-347 1.04e-04

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: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 179 EGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMI 258
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 259 AMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRgrgpppgAEEKEKEpdgvdLLSELRAENQRLTASLQ 338
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAE-----EEAELEEEEEALLELLA 466


                  ....*....
gi 1958789722 339 ELQEGLQQE 347
Cdd:COG1196   467 ELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-407 1.30e-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: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  194 EARKSQLHRE-QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymIAMRLAQLSEEKNSa 272
Cdd:TIGR02168  273 RLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE---LAEELAELEEKLEE- 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  273 vlrsrdLQLAVDQLKLKVSRLEEECALLRRGRGPPpgAEEKEKEPDGVDLLSE----LRAENQRLTASLQELQEGLQQEM 348
Cdd:TIGR02168  349 ------LKEELESLEAELEELEAELEELESRLEEL--EEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRRERLQ 420

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789722  349 SRPGAAGSERILLDILEHDWR---------EAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 407
Cdd:TIGR02168  421 QEIEELLKKLEEAELKELQAEleeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-407 1.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  187 TEVRRLREARKSQLHRE--QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAgslELLRLKDEnymiamRLAQ 264
Cdd:COG4913    272 AELEYLRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNGGD------RLEQ 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  265 LSEEKnsavlrsRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgaeeKEKEPDGVDLLSELRAENQRLTASLQELQEGL 344
Cdd:COG4913    343 LEREI-------ERLERELEERERRRARLEALLAAL------------GLPLPASAEEFAALRAEAAALLEALEEELEAL 403

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789722  345 QQEMsrpgaagserilldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 407
Cdd:COG4913    404 EEAL--------------------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-498 2.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRR-----------------------------------GRGPPPGAEE 312
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaarllllleaeadyegflegvkaalllaglRGLAGAVAVL 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 313 --KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQ 390
Cdd:COG1196   530 igVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 391 WAEELRDKYLQEMEDLRLKHRTLlkdcDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLE 470
Cdd:COG1196   610 EADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685

                         330       340
                  ....*....|....*....|....*...
gi 1958789722 471 AERDELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:COG1196   686 ERLAEEELELEEALLAEEEEERELAEAE 713
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
188-366 2.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENymiamRLAQLSE 267
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-----RFAAALG 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  268 EKNSAVLRsRDLQLAVDQLKLKVSRLEEECALLRRG---RGPPPGAE---EKEKEPDGVDLLSELRAEN---------QR 332
Cdd:COG4913    761 DAVERELR-ENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADldaDLESLPEYLALLDRLEEDGlpeyeerfkEL 839

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958789722  333 LTASLQELQEGLQQEMSRPGAAGSERI--LLDILEH 366
Cdd:COG4913    840 LNENSIEFVADLLSKLRRAIREIKERIdpLNDSLKR 875
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-423 5.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  170 SMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLqargRALEEERAGLE--QRLREQQAAQERCQRLREDWEAgSLE 247
Cdd:COG4913    215 EYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAEryAAARERLAELEYLRAALRLWFA-QRR 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  248 LLRLKDEnymiamrLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallRRGrgpppgaeekekepDGVDLLSELR 327
Cdd:COG4913    290 LELLEAE-------LEELRAELARLEAELERLEARLDALREELDELEAQ----IRG--------------NGGDRLEQLE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  328 AENQRLTASLQELQEGLQQEMSRPGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 407
Cdd:COG4913    345 REIERLERELEERERRRARLEALLAALGLP------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                          250
                   ....*....|....*.
gi 1958789722  408 LKHRTLLKDCDLYKHR 423
Cdd:COG4913    419 RELRELEAEIASLERR 434
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-491 5.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 173 LDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLK 252
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 253 DENymiamrlaQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEP-DGVDLLSELRAENQ 331
Cdd:COG4717   241 LEE--------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaSLGKEAEELQALPA 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 332 RLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHR 411
Cdd:COG4717   313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 412 TLLKDCDLyKHRMATVLAQLEEIEKERDQAIQSRDRIQLQysqslIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLE 491
Cdd:COG4717   393 QAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEEELEELREELAELEAELEQLE 466
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 190-495 6.23e-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: 43.13  E-value: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  190 RRLREARKSQLHREQQlqargrALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymIAMRLAQLSEEk 269
Cdd:TIGR02169  218 KEKREYEGYELLKEKE------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE---LNKKIKDLGEE- 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  270 nsavlRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEms 349
Cdd:TIGR02169  288 -----EQLRVKEKIGELEAEIASLERSIAEKERE------LEDAEER------LAKLEAEIDKLLAEIEELEREIEEE-- 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  350 rpgaagseRILLDILEHDWREAQDSRQELCQKLHAVQGELQ-WAEELR------DKYLQEMEDL-----RLKHRTLLKDC 417
Cdd:TIGR02169  349 --------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKdyreklEKLKREINELkreldRLQEELQRLSE 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  418 DLYKHRM--ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQ 495
Cdd:TIGR02169  421 ELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
320-476 7.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  320 VDLLSELRAENQRLTASLQELQEG-LQQEMSRPGAAGSERILL----DILEHDWREAQDSRQELCQKLHAVQGELqwaEE 394
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELeYLRAALRLWFAQRRLELLeaelEELRAELARLEAELERLEARLDALREEL---DE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  395 LRDKYLQ-----------EMEDLRLKHRTLLKDCDLYKHRMATV-----------LAQLEEIEKERDQAIQSRDRIQLQY 452
Cdd:COG4913    328 LEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEAL 407

                          170       180
                   ....*....|....*....|....
gi 1958789722  453 SQSLIEKDQYRKQVRGLEAERDEL 476
Cdd:COG4913    408 AEAEAALRDLRRELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
376-494 7.46e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  376 QELCQKLHAVQGELQWAEELRDKylQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQS 455
Cdd:COG4913    258 RELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958789722  456 -LIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQL 494
Cdd:COG4913    336 gGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
169-476 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 169 CSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGlEQRLREQQAAQERCQRLREDWEAGSLEL 248
Cdd:PRK03918  441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEE 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 249 LRLKDENYmiamrlaqlseEKnsavLRSRDLQLAVDQLKLKvSRLEEECALLRRGRGPPPGAEEKEKEPDgvDLLSELRA 328
Cdd:PRK03918  520 LEKKAEEY-----------EK----LKEKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELA--ELLKELEE 581

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 329 EN----QRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE-M 403
Cdd:PRK03918  582 LGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeY 661

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789722 404 EDLRLKHRTLLKdcdlykhRMATVLAQLEEIEKERDQAIQSRDRIQLQysqsLIEKDQYRKQVRGLEAERDEL 476
Cdd:PRK03918  662 EELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERV 723
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
186-413 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 186 MTEVRRLREARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQERCQRlredweagSLELLRLKDENYMIAMRLAQL 265
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE--------ELEKLEKLLQLLPLYQELEAL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 266 SEEknsavlrsrdlqlavdqLKLKVSRLEEecallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 345
Cdd:COG4717   138 EAE-----------------LAELPERLEE--------------LEERLEE------LRELEEELEELEAELAELQEELE 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789722 346 QEMSRPGAAgserilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTL 413
Cdd:COG4717   181 ELLEQLSLA---------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 186-493 2.31e-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: 41.26  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  186 MTEVRRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRlaql 265
Cdd:pfam15921  333 LREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR---- 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  266 sEEKNSAVLRSrdLQLAVDQLKLKVSRLEeecALLRRGRGPPPGaeEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQ 345
Cdd:pfam15921  407 -DTGNSITIDH--LRRELDDRNMEVQRLE---ALLKAMKSECQG--QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  346 QEMSRPGAagsERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH---RTLLKDCDLYKH 422
Cdd:pfam15921  479 KVVEELTA---KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKL 555

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789722  423 RMA-------TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQ 493
Cdd:pfam15921  556 QMAekdkvieILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-484 2.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 191 RLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK- 269
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEl 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 270 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVD-LLSELRAENQRLTASLQELQEGLQQEM 348
Cdd:COG4717   195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKeARLLLLIAAALLALLGLGGSLLSLILT 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 349 SRPGAAGSERILLDILEHDWREAQDSRQELcQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVL 428
Cdd:COG4717   275 IAGVLFLVLGLLALLFLLLAREKASLGKEA-EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958789722 429 AQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEaERDELLTTVTSLE 484
Cdd:COG4717   354 REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELE 408
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 164-491 2.86e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  164 EPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEEraglEQRLREQQAAQERC-QRLREDWE 242
Cdd:TIGR00618  512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCdNRSKEDIP 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  243 AGSLELLRLKDENYMIAMRLAQLSEEkNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDL 322
Cdd:TIGR00618  588 NLQNITVRLQDLTEKLSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  323 LSELRAEN-QRLTASLQELQEGLQQEMS-RPGAAGSERILLDILEHDwREAQDSRQELCQKLHAVQGELQWAEELRDKYL 400
Cdd:TIGR00618  667 IRVLPKELlASRQLALQKMQSEKEQLTYwKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDALNQSL 745

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  401 QEMEDLR---LKHRTLLKDCDLYKHRMA-TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDEL 476
Cdd:TIGR00618  746 KELMHQArtvLKARTEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET 825

                          330
                   ....*....|....*
gi 1958789722  477 LttVTSLEGTKAMLE 491
Cdd:TIGR00618  826 L--VQEEEQFLSRLE 838
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
290-473 4.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 290 VSRLEEECALLRRGRGPPP-----GAEEKEKEpdgVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDIL 364
Cdd:COG4717    48 LERLEKEADELFKPQGRKPelnlkELKELEEE---LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722 365 E------HDWREAQDSRQELCQKLHAVQGELQWAEELRDKY---LQEMEDLRLKHRTLLKDCDLYKH-RMATVLAQLEEI 434
Cdd:COG4717   125 LqllplyQELEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEeELQDLAEELEEL 204

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958789722 435 EKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 473
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-442 4.74e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAA----QERCQRLREDWEAGSLELLRLKDENYMIAMRLA 263
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  264 QLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALL--RRGRgpppgaEEKEKEPDGVDLLSELRAENQRLTASLQELQ 341
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedRRER------LQQEIEELLKKLEEAELKELQAELEELEEEL 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  342 EGLQQEMSRPGAAgserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR--LKHRTLLKDcdl 419
Cdd:TIGR02168  450 EELQEELERLEEA------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSG--- 520

                          250       260
                   ....*....|....*....|...
gi 1958789722  420 ykhrMATVLAQLEEIEKERDQAI 442
Cdd:TIGR02168  521 ----ILGVLSELISVDEGYEAAI 539
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 176-268 7.82e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789722  176 EGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLRE----QQAAQERCQRLREDWEAGSLE-LLR 250
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEleekQQELEAQLEQLQEKAAETSQErKQK 217

                           90
                   ....*....|....*...
gi 1958789722  251 LKDENYMIAMRLaQLSEE 268
Cdd:PRK11448   218 RKEITDQAAKRL-ELSEE 234
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 78-150 9.13e-03

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 36.03  E-value: 9.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789722  78 ERIEGVRHRLTRALNPAKLTPYLRQCrvLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRG-FEAFLEALE 150
Cdd:pfam16739   7 RLLRLFRPRLKDTIKPTEILPHLPEC--LTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGwFRAFLDALR 78
 
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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