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Conserved domains on  [gi|194474088|ref|NP_001124026|]
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caspase recruitment domain-containing protein 10 [Rattus norvegicus]

Protein Classification

BAR and SH3 domains-containing protein; SH3 domain-containing protein( domain architecture ID 12962297)

BAR (Bin/Amphiphysin/Rvs) and SH3 (Src homology 3) domain-containing protein| SH3 (SRC Homology 3) domain-containing protein similar to Escherichia coli uncharacterized protein YgiM; SH3 domains are protein interaction domains that bind proline-rich ligands

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 ...
27-112 2.52e-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: 180.49  E-value: 2.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08807    81 HFTLLT 86
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-450 1.75e-14

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: 78.44  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 298
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  299 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 378
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194474088  379 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
696-761 7.52e-05

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd12026:

Pssm-ID: 473055  Cd Length: 65  Bit Score: 41.60  E-value: 7.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088  696 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 761
Cdd:cd12026     1 DSFYIRTHFEY-EKESPYGLSFNKGEVFRVVDTLYNgKLGSWLAIRIGK-NHKEVERGIIPNKNRAE 65
 
Name Accession Description Interval E-value
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
27-112 2.52e-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: 180.49  E-value: 2.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08807    81 HFTLLT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
28-114 7.52e-16

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: 73.36  E-value: 7.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088    28 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 194474088   107 HFTLLTGQ 114
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-450 1.75e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 298
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  299 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 378
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194474088  379 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-450 2.61e-11

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: 68.16  E-value: 2.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   144 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 223
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   224 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 303
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   304 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 383
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088   384 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
mukB PRK04863
chromosome partition protein MukB;
155-435 7.96e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  155 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdweagSLELLRLKDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 232
Cdd:PRK04863  844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR-----LLPRLNLLADETLAD-RVEEIREQLDEAEEAKRFVQQh 916
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  233 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 301
Cdd:PRK04863  917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  302 pgaAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 381
Cdd:PRK04863  997 ---AEQER---TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194474088  382 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 435
Cdd:PRK04863 1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
153-453 3.58e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   153 REQQLQARGRALEEERAGLEQRLREQQAAQERCQ--RLREDWEAGSLE--LLRLKDENY-------MIAMRLAQLS---- 217
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQleKVTTEAKIKKLEedILLLEDQNSklskerkLLEERISEFTsnla 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   218 --EEKNSAVLRSRDLQLAV-----DQLKlKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSELRAENQRLTASLQE 290
Cdd:pfam01576  170 eeEEKAKSLSKLKNKHEAMisdleERLK-KEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   291 LQEGLQQEMSRPGAAGS-----ERILLDILEHDWRE------AQDSRQELCQKLHAVQGELQ-------WAEELRDKYLQ 352
Cdd:pfam01576  248 ALARLEEETAQKNNALKkirelEAQISELQEDLESEraarnkAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQ 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   353 EMEDLRlkhRTLLKDCDLYKhrmatvlAQLEEIEKERDQAIqsrDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVT 432
Cdd:pfam01576  328 EVTELK---KALEEETRSHE-------AQLQEMRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
                          330       340
                   ....*....|....*....|....*...
gi 194474088   433 SLEGTKA-------MLEAQLQRTQGGSS 453
Cdd:pfam01576  395 TLQQAKQdsehkrkKLEGQLQELQARLS 422
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
696-761 7.52e-05

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212959  Cd Length: 65  Bit Score: 41.60  E-value: 7.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088  696 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 761
Cdd:cd12026     1 DSFYIRTHFEY-EKESPYGLSFNKGEVFRVVDTLYNgKLGSWLAIRIGK-NHKEVERGIIPNKNRAE 65
 
Name Accession Description Interval E-value
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
27-112 2.52e-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: 180.49  E-value: 2.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08807     1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08807    81 HFTLLT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
27-112 1.05e-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: 141.36  E-value: 1.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPcrANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08785     1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08785    79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
27-112 9.92e-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: 130.13  E-value: 9.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08808     1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08808    81 LYKLVT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
27-112 3.44e-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: 97.25  E-value: 3.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08806     1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                  ....*.
gi 194474088  107 HFTLLT 112
Cdd:cd08806    81 LYTQVT 86
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
28-112 5.86e-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: 96.53  E-value: 5.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   28 WERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 107
Cdd:cd08809     2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81

                  ....*
gi 194474088  108 FTLLT 112
Cdd:cd08809    82 YKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
28-114 7.52e-16

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: 73.36  E-value: 7.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088    28 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 194474088   107 HFTLLTGQ 114
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-450 1.75e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 298
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  299 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 378
Cdd:COG1196   370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194474088  379 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
35-107 7.47e-12

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: 61.76  E-value: 7.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194474088   35 RHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 107
Cdd:cd01671     5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE---KTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPH 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-450 2.61e-11

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: 68.16  E-value: 2.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   144 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 223
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   224 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 303
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   304 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 383
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088   384 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
114-449 5.93e-11

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: 67.02  E-value: 5.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   114 QEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQrlrEQQAAQERCQRLREDWE 193
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ---EEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   194 AGSLELLRLKDENYMIAMRLAQLSEEKNsavlrsrdlqlavdQLKLKVSRLEEEcallrrgrgpppgaEEKEKEPDGVDL 273
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLH--------------KLEEALNDLEAR--------------LSHSRIPEIQAE 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   274 LSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE 353
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   354 MEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLttvtS 433
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL----S 952
                          330
                   ....*....|....*.
gi 194474088   434 LEGTKAMLEAQLQRTQ 449
Cdd:TIGR02169  953 LEDVQAELQRVEEEIR 968
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-435 1.83e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  141 RRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 220
Cdd:COG1196   262 LAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaeekekepdgVDLLSELRAENQRLTASLQELQEGLQQEMS 300
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---------------AEAEEELEELAEELLEALRAAAELAAQLEE 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  301 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 380
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194474088  381 QLEEiEKERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDELLTTVTSLE 435
Cdd:COG1196   485 ELAE-AAARLLLLLEAEADYEGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYE 537
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
29-101 1.98e-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: 55.05  E-value: 1.98e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194474088   29 ERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALE 101
Cdd:cd08810     3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR---TTRKKRVDKLLDILAREGPDGLDALIESIR 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
173-449 3.11e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  173 QRLREQQAAQERCQRLREDWEAGSLELLRLKDENymIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallr 252
Cdd:COG1196   203 EPLERQAEKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLE----- 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  253 rgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWRE----AQDSRQE 328
Cdd:COG1196   276 --------LEELELE------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEELEE 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  329 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLI 408
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 194474088  409 EKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
124-437 2.01e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   124 LDEEGPEGLTQF--LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRL-----------REQQAAQERCQRLRE 190
Cdd:TIGR02168  717 LRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeeelaeaeAEIEELEAQIEQLKE 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   191 DWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGppPGAEEKEKEPDG 270
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--ELEELIEELESE 874
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   271 VDLLSELRAENQRLTASLQELQEGLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDkY 350
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEE-------------LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-N 940
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   351 LQEMedLRLKHRTLLKDcdlykhrmatVLAQLEEIEKERDQAIQSRDRIQLQYSQ-------SLIEKDQYRKQVRGLEAE 423
Cdd:TIGR02168  941 LQER--LSEEYSLTLEE----------AEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
                          330
                   ....*....|....
gi 194474088   424 RDELLTTVTSLEGT 437
Cdd:TIGR02168 1009 KEDLTEAKETLEEA 1022
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
142-450 2.53e-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: 55.06  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   142 RLREARKsQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELL-----RLKDENYMIAMRLAQL 216
Cdd:TIGR02168  173 RRKETER-KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEA 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   217 SEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 296
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEE-------------IEELQKE------LYALANEISRLEQQKQILRERLA 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   297 QeMSRPGAAGSERIL-----LDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLY 371
Cdd:TIGR02168  313 N-LERQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474088   372 KHRMATVLAQLEEIEKERDQAIQSRDRiqLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
140-405 3.01e-06

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: 51.49  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  140 VRRLREARK----SQLH------REQQLQARGRALEEERAGLEQRLREQQAAQERCQRL------------RED-WEAGS 196
Cdd:COG3096   419 VQALEKARAlcglPDLTpenaedYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQaWQTAR 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  197 lELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKlkvsrleeecALLRRGRGPPPGAEEKEkepdgvDLLSE 276
Cdd:COG3096   499 -ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----------EFCQRIGQQLDAAEELE------ELLAE 561
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  277 LRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQklhavqgelQWAEELRDkyLQEMED 356
Cdd:COG3096   562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE---------QSGEALAD--SQEVTA 630
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 194474088  357 LrlkhrtllkdcdlykhrMATVLAQLEEIEKERDQAIQSRDRIQLQYSQ 405
Cdd:COG3096   631 A-----------------MQQLLEREREATVERDELAARKQALESQIER 662
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-427 3.68e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  138 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEA-----------GSLELLRLKDEN 206
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalllaglrglaGAVAVLIGVEAA 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  207 YMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLK-LKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAENQRLT 285
Cdd:COG1196   536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  286 ASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQD-----------SRQELCQKLHAVQGELQWAEELRDKYLQEM 354
Cdd:COG1196   616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggSRRELLAALLEAEAELEELAERLAEEELEL 695
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  355 EDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEK-----------DQYRKQVRGLEAE 423
Cdd:COG1196   696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELERLERE 775

                  ....
gi 194474088  424 RDEL 427
Cdd:COG1196   776 IEAL 779
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
162-435 4.88e-06

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: 50.72  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  162 RALEEERAGLEQRLrEQQAAQERCQRLREDWEAGSLELLR--------LKDENymIAMRLAQLSEEKNSAvlrsRDLQLA 233
Cdd:COG3096   839 AALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADET--LADRLEELREELDAA----QEAQAF 911
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  234 VDQLKLKVSRLEEECALLRRgrgpPPGAEEkekepdgvdllsELRAENQRLTASLQELQEG---LQQEMSR--------- 301
Cdd:COG3096   912 IQQHGKALAQLEPLVAVLQS----DPEQFE------------QLQADYLQAKEQQRRLKQQifaLSEVVQRrphfsyeda 975
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  302 PGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELqwaeelrDKYLQEMEDLRLKHRTllkdcdlyKHRMATVLAQ 381
Cdd:COG3096   976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLASLKSSRDA--------KQQTLQELEQ 1040
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  382 -LEEIEKERD-----QAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 435
Cdd:COG3096  1041 eLEELGVQADaeaeeRARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
162-447 5.91e-06

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: 50.45  E-value: 5.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   162 RALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDenymiamRLAQLSEEKNSAvLRSRDLQLAVDQLKLKV 241
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRREREKA-ERYQALLKEKREYEGYE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   242 SRLEEEcallrrgrgpppgAEEKEKEpdgvdllsELRAENQRLTASLQELQEGLQQEMSRPGAAgsERILLDILEHDWRE 321
Cdd:TIGR02169  228 LLKEKE-------------ALERQKE--------AIERQLASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDL 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   322 AQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQ---AIQSRD- 397
Cdd:TIGR02169  285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKe 364
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   398 -----RIQLQ-----YSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 447
Cdd:TIGR02169  365 eledlRAELEevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-301 6.10e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  141 RRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQERCQRLRE------DWEAGSLELLRLKDE-------NY 207
Cdd:COG4913   609 RAKLAALEAEL---AELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAElerldasSD 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  208 MIA---MRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAEN--Q 282
Cdd:COG4913   686 DLAaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAveR 765
                         170
                  ....*....|....*....
gi 194474088  283 RLTASLQELQEGLQQEMSR 301
Cdd:COG4913   766 ELRENLEERIDALRARLNR 784
mukB PRK04863
chromosome partition protein MukB;
155-435 7.96e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  155 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdweagSLELLRLKDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 232
Cdd:PRK04863  844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR-----LLPRLNLLADETLAD-RVEEIREQLDEAEEAKRFVQQh 916
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  233 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 301
Cdd:PRK04863  917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  302 pgaAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 381
Cdd:PRK04863  997 ---AEQER---TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194474088  382 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 435
Cdd:PRK04863 1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
145-450 1.08e-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: 49.67  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   145 EARKSQLHRE-QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrlaqlseeknsa 223
Cdd:TIGR02168  273 RLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE------------------ 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   224 vlrsrdLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLQQEMSRpg 303
Cdd:TIGR02168  335 ------LAEELAELEEKLEELKEELESLE-------------------AELEELEAELEELESRLEELEEQLETLRSK-- 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   304 aagserilLDILEHDWREAQDSRQELCQKLHAVQGElqwaeelRDKYLQEMEDLRLKhrtllkdcdLYKHRMATVLAQLE 383
Cdd:TIGR02168  388 --------VAQLELQIASLNNEIERLEARLERLEDR-------RERLQQEIEELLKK---------LEEAELKELQAELE 443
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088   384 EIEKERDQAIQSRDRIQLQYSQSliekdqyRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEEL-------REELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
mukB PRK04863
chromosome partition protein MukB;
143-245 2.54e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  143 LREARkSQLHREQQLQARGRALEEeragLEQRLREQQAAQER----CQRLREDWEAGS-LELLRLKDEnymiaMRLAQLS 217
Cdd:PRK04863  502 LRRLR-EQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLlaefCKRLGKNLDDEDeLEQLQEELE-----ARLESLS 571
                          90       100
                  ....*....|....*....|....*...
gi 194474088  218 EEKNSAVLRSRDLQLAVDQLKLKVSRLE 245
Cdd:PRK04863  572 ESVSEARERRMALRQQLEQLQARIQRLA 599
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
141-446 2.72e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   141 RRLREARKSQLHREQQlqargrALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymIAMRLAQLSEEk 220
Cdd:TIGR02169  218 KEKREYEGYELLKEKE------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE---LNKKIKDLGEE- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   221 nsavlRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEms 300
Cdd:TIGR02169  288 -----EQLRVKEKIGELEAEIASLERSIAEKERE------LEDAEER------LAKLEAEIDKLLAEIEELEREIEEE-- 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   301 rpgaagseRILLDILEHDWREAQDSRQELCQKLHAVQGELQ-WAEELR------DKYLQEMEDL-----RLKHRTLLKDC 368
Cdd:TIGR02169  349 --------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKdyreklEKLKREINELkreldRLQEELQRLSE 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   369 DLYKHRM--ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQ 446
Cdd:TIGR02169  421 ELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-358 2.95e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  138 TEVRRLREARKSQLHRE--QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAgslELLRLKDEnymiamRLAQ 215
Cdd:COG4913   272 AELEYLRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNGGD------RLEQ 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  216 LSEEKnsavlrsRDLQLAVDQLKLKVSRLEEECALLrrGRGPPPGAEEkekepdgvdlLSELRAENQRLTASLQELQEGL 295
Cdd:COG4913   343 LEREI-------ERLERELEERERRRARLEALLAAL--GLPLPASAEE----------FAALRAEAAALLEALEEELEAL 403
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194474088  296 QQEMsrpgaagserilldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 358
Cdd:COG4913   404 EEAL--------------------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
130-298 2.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  130 EGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMI 209
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  210 AMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRgrgpppgAEEKEKEpdgvdLLSELRAENQRLTASLQ 289
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAE-----EEAELEEEEEALLELLA 466

                  ....*....
gi 194474088  290 ELQEGLQQE 298
Cdd:COG1196   467 ELLEEAALL 475
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
153-453 3.58e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   153 REQQLQARGRALEEERAGLEQRLREQQAAQERCQ--RLREDWEAGSLE--LLRLKDENY-------MIAMRLAQLS---- 217
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQleKVTTEAKIKKLEedILLLEDQNSklskerkLLEERISEFTsnla 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   218 --EEKNSAVLRSRDLQLAV-----DQLKlKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSELRAENQRLTASLQE 290
Cdd:pfam01576  170 eeEEKAKSLSKLKNKHEAMisdleERLK-KEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   291 LQEGLQQEMSRPGAAGS-----ERILLDILEHDWRE------AQDSRQELCQKLHAVQGELQ-------WAEELRDKYLQ 352
Cdd:pfam01576  248 ALARLEEETAQKNNALKkirelEAQISELQEDLESEraarnkAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQ 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   353 EMEDLRlkhRTLLKDCDLYKhrmatvlAQLEEIEKERDQAIqsrDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVT 432
Cdd:pfam01576  328 EVTELK---KALEEETRSHE-------AQLQEMRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
                          330       340
                   ....*....|....*....|....*...
gi 194474088   433 SLEGTKA-------MLEAQLQRTQGGSS 453
Cdd:pfam01576  395 TLQQAKQdsehkrkKLEGQLQELQARLS 422
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-449 3.86e-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: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRR-----------------------------------GRGPPPGAEE 263
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaarllllleaeadyegflegvkaalllaglRGLAGAVAVL 529
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  264 --KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQ 341
Cdd:COG1196   530 igVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  342 WAEELRDKYLQEMEDLRLKHRTLlkdcDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLE 421
Cdd:COG1196   610 EADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
                         330       340
                  ....*....|....*....|....*...
gi 194474088  422 AERDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG1196   686 ERLAEEELELEEALLAEEEEERELAEAE 713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
137-362 3.96e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  137 MTEVRRLREARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQERCQRlredweagSLELLRLKDENYMIAMRLAQL 216
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE--------ELEKLEKLLQLLPLYQELEAL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  217 SEEknsavlrsrdlqlavdqLKLKVSRLEEecallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 296
Cdd:COG4717   138 EAE-----------------LAELPERLEE--------------LEERLEE------LRELEEELEELEAELAELQEELE 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194474088  297 QEMSRPGAAGSERiLLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHR 362
Cdd:COG4717   181 ELLEQLSLATEEE-LQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-442 4.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSL-ELLRLKDENYMIAMRLAQLS 217
Cdd:COG4717   133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELE 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  218 EEKNSAVLRSRDLQLAVDQLKLKVSRLEEE----------------CALLRRGRGPPPGAEE------------------ 263
Cdd:COG4717   213 EELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalLALLGLGGSLLSLILTiagvlflvlgllallfll 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  264 -KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQW 342
Cdd:COG4717   293 lAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  343 AEELRDKYLQEMEDLRLKHRTLLKDCDLyKHRMATVLAQLEEIEKERDQAIQSRDRIQLQysqslIEKDQYRKQVRGLEA 422
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEE 446
                         330       340
                  ....*....|....*....|
gi 194474088  423 ERDELLTTVTSLEGTKAMLE 442
Cdd:COG4717   447 ELEELREELAELEAELEQLE 466
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
115-442 6.78e-05

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: 46.89  E-value: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   115 EPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEEraglEQRLREQQAAQERC-QRLREDWE 193
Cdd:TIGR00618  512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCdNRSKEDIP 587
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   194 AGSLELLRLKDENYMIAMRLAQLSEEkNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDL 273
Cdd:TIGR00618  588 NLQNITVRLQDLTEKLSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   274 LSELRAEN-QRLTASLQELQEGLQQEMS-RPGAAGSERILLDILEH---DWREaqdsRQELCQKLHAVQGELQWAEELRD 348
Cdd:TIGR00618  667 IRVLPKELlASRQLALQKMQSEKEQLTYwKEMLAQCQTLLRELETHieeYDRE----FNEIENASSSLGSDLAAREDALN 742
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   349 KYLQEMEDLR---LKHRTLLKDCDLYKHRMA-TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:TIGR00618  743 QSLKELMHQArtvLKARTEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
                          330
                   ....*....|....*...
gi 194474088   425 DELLttVTSLEGTKAMLE 442
Cdd:TIGR00618  823 CETL--VQEEEQFLSRLE 838
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-317 6.84e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENymiamRLAQLSE 218
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-----RFAAALG 760
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EKNSAVLRsRDLQLAVDQLKLKVSRLEEECALLRRG---RGPPPGAE---EKEKEPDGVDLLSELRAEN---------QR 283
Cdd:COG4913   761 DAVERELR-ENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADldaDLESLPEYLALLDRLEEDGlpeyeerfkEL 839
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 194474088  284 LTASLQELQEGLQQEMSRPGAAGSERI--LLDILEH 317
Cdd:COG4913   840 LNENSIEFVADLLSKLRRAIREIKERIdpLNDSLKR 875
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
696-761 7.52e-05

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212959  Cd Length: 65  Bit Score: 41.60  E-value: 7.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194474088  696 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 761
Cdd:cd12026     1 DSFYIRTHFEY-EKESPYGLSFNKGEVFRVVDTLYNgKLGSWLAIRIGK-NHKEVERGIIPNKNRAE 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-427 7.64e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 7.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  120 CSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGlEQRLREQQAAQERCQRLREDWEAGSLEL 199
Cdd:PRK03918  441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEE 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  200 LRLKDENYmiamrlaqlseEKnsavLRSRDLQLAVDQLKLKvSRLEEECALLRRGRGPPPGAEEKEKEPDgvDLLSELRA 279
Cdd:PRK03918  520 LEKKAEEY-----------EK----LKEKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELA--ELLKELEE 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  280 EN----QRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE-M 354
Cdd:PRK03918  582 LGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeY 661
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194474088  355 EDLRLKHRTLLKdcdlykhRMATVLAQLEEIEKERDQAIQSRDRIQLQysqsLIEKDQYRKQVRGLEAERDEL 427
Cdd:PRK03918  662 EELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERV 723
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
699-761 7.91e-05

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212793  Cd Length: 62  Bit Score: 41.51  E-value: 7.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194474088  699 YIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 761
Cdd:cd11859     1 YIRTHFDY-EKPAKGELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
137-444 1.32e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.26  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   137 MTEVRRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRlaql 216
Cdd:pfam15921  333 LREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR---- 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   217 sEEKNSAVLRSrdLQLAVDQLKLKVSRLEeecALLRRGRGPPPGAEEKEkepdgvdlLSELRAENQ------RLTASLQE 290
Cdd:pfam15921  407 -DTGNSITIDH--LRRELDDRNMEVQRLE---ALLKAMKSECQGQMERQ--------MAAIQGKNEslekvsSLTAQLES 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   291 LQEGLQQEMSRPGAagsERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH---RTLLKD 367
Cdd:pfam15921  473 TKEMLRKVVEELTA---KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTE 549
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   368 CDLYKHRMA-------TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAM 440
Cdd:pfam15921  550 CEALKLQMAekdkvieILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629

                   ....
gi 194474088   441 LEAQ 444
Cdd:pfam15921  630 LELE 633
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-374 1.35e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  121 SMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLqargRALEEERAGLE--QRLREQQAAQERCQRLREDWEAgSLE 198
Cdd:COG4913   215 EYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAEryAAARERLAELEYLRAALRLWFA-QRR 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  199 LLRLKDEnymiamrLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallRRGrgpppgaeekekepDGVDLLSELR 278
Cdd:COG4913   290 LELLEAE-------LEELRAELARLEAELERLEARLDALREELDELEAQ----IRG--------------NGGDRLEQLE 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  279 AENQRLTASLQELQEGLQQEMSRPGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 358
Cdd:COG4913   345 REIERLERELEERERRRARLEALLAALGLP------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
                         250
                  ....*....|....*.
gi 194474088  359 LKHRTLLKDCDLYKHR 374
Cdd:COG4913   419 RELRELEAEIASLERR 434
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-449 1.66e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAgSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEELEE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  219 EknsaVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgppPGAEEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQQ- 297
Cdd:COG4717   154 R----LEELRELEEELEELEAELAELQEELEELLEQ----LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEl 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  298 -------EMSRPGAAGSERI-----------LLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRL 359
Cdd:COG4717   226 eeeleqlENELEAAALEERLkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  360 KHRTLLKDCDLYKHRMATVLAQLE-EIEKERDQAIQSRDRI-QLQYSQSLIEKDQYRKQVRGLEAERDELLTT--VTSLE 435
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEagVEDEE 385
                         330
                  ....*....|....
gi 194474088  436 GTKAMLEAQLQRTQ 449
Cdd:COG4717   386 ELRAALEQAEEYQE 399
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
271-427 2.09e-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: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  271 VDLLSELRAENQRLTASLQELQEgLQQEMSRPGAAGSERIL------LDILEHDWREAQDSRQELCQKLHAVQGELqwaE 344
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQRRLelleaeLEELRAELARLEAELERLEARLDALREEL---D 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  345 ELRDKYLQ-----------EMEDLRLKHRTLLKDCDLYKHRMATV-----------LAQLEEIEKERDQAIQSRDRIQLQ 402
Cdd:COG4913   327 ELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEA 406
                         170       180
                  ....*....|....*....|....*
gi 194474088  403 YSQSLIEKDQYRKQVRGLEAERDEL 427
Cdd:COG4913   407 LAEAEAALRDLRRELRELEAEIASL 431
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
141-475 2.97e-04

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: 44.96  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   141 RRLREARKSQLHREQQLQARGRALEEERAgLEQRLREQQAAQERcqrlREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 220
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRARIEELRA-QEAVLEETQERINR----ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   221 NS-AVLRSRDLQLAVDQLKLKVSR-----LEEECALLRRGRGPPPG-AEEKEKEpdgVDLLSELRAENQRLTASLQELQe 293
Cdd:TIGR00618  321 RSrAKLLMKRAAHVKQQSSIEEQRrllqtLHSQEIHIRDAHEVATSiREISCQQ---HTLTQHIHTLQQQKTTLTQKLQ- 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   294 glqqemsrpgAAGSERILLDILEHDwREAQDSRQE-LCQKLHAVQGElqwaEELRDKYLQEMEDLRLKHRTLLKDCDLYK 372
Cdd:TIGR00618  397 ----------SLCKELDILQREQAT-IDTRTSAFRdLQGQLAHAKKQ----QELQQRYAELCAAAITCTAQCEKLEKIHL 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   373 HRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR-TQGG 451
Cdd:TIGR00618  462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLE 541
                          330       340
                   ....*....|....*....|....
gi 194474088   452 SSLKacASSHSLCSNLSSTWSLSE 475
Cdd:TIGR00618  542 TSEE--DVYHQLTSERKQRASLKE 563
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
142-449 3.05e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  142 RLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK- 220
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEl 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVD-LLSELRAENQRLTASLQELQEGLQQEM 299
Cdd:COG4717   195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKeARLLLLIAAALLALLGLGGSLLSLILT 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  300 SRPGAAGSERILLDILEHDWREAQDSRQELcQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVL 379
Cdd:COG4717   275 IAGVLFLVLGLLALLFLLLAREKASLGKEA-EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  380 AQLEEIEKERDQAIQSRDRIQL----------QYSQSLIEKDQY---RKQVRGLEAERDELLTTVTSL--EGTKAMLEAQ 444
Cdd:COG4717   354 REAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYqelKEELEELEEQLEELLGELEELleALDEEELEEE 433

                  ....*
gi 194474088  445 LQRTQ 449
Cdd:COG4717   434 LEELE 438
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
241-424 3.80e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  241 VSRLEEECALLRRGRGPPP-----GAEEKEKEpdgVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDIL 315
Cdd:COG4717    48 LERLEKEADELFKPQGRKPelnlkELKELEEE---LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  316 E------HDWREAQDSRQELCQKLHAVQGELQWAEELRDKY---LQEMEDLRLKHRTLLKDCDLYKH-RMATVLAQLEEI 385
Cdd:COG4717   125 LqllplyQELEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEeELQDLAEELEEL 204
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 194474088  386 EKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
327-445 3.82e-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: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  327 QELCQKLHAVQGELQWAEELRDKylQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQS 406
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 194474088  407 -LIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQL 445
Cdd:COG4913   336 gGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
698-761 5.15e-04

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212961  Cd Length: 65  Bit Score: 39.47  E-value: 5.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474088  698 FYIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 761
Cdd:cd12028     3 FYIRTHFDY-EPDPPSGLSFTRGEVFHVLDTMHRGKlGSWLAVRMGR-DLREMEKGIIPNQSRAE 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
139-393 5.65e-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: 43.89  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAA----QERCQRLREDWEAGSLELLRLKDENYMIAMRLA 214
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   215 QLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALL--RRGRgpppgaEEKEKEPDGVDLLSELRAENQRLTASLQELQ 292
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedRRER------LQQEIEELLKKLEEAELKELQAELEELEEEL 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   293 EGLQQEMSRPGAAgserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR--LKHRTLLKDCDl 370
Cdd:TIGR02168  450 EELQEELERLEEA------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSGIL- 522
                          250       260
                   ....*....|....*....|...
gi 194474088   371 ykhrmaTVLAQLEEIEKERDQAI 393
Cdd:TIGR02168  523 ------GVLSELISVDEGYEAAI 539
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
261-412 6.58e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 6.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   261 AEEKEKEPDGVDLLSELRAENQRLTASLQELQ---EGLQQEMsrpgaAGSER---IL------LDILEHDWREAQDSRQE 328
Cdd:pfam13851   36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQeevEELRKQL-----ENYEKdkqSLknlkarLKVLEKELKDLKWEHEV 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   329 LCQKLHAVQGELQwaeELRDKYLQEMEDLRLKhrTLLKDCdLYKHRMATVLAQLEEIEKERDQAIQS-------RDRIQL 401
Cdd:pfam13851  111 LEQRFEKVERERD---ELYDKFEAAIQDVQQK--TGLKNL-LLEKKLQALGETLEKKEAQLNEVLAAanldpdaLQAVTE 184
                          170
                   ....*....|.
gi 194474088   402 QYSQSLIEKDQ 412
Cdd:pfam13851  185 KLEDVLESKNQ 195
PTZ00121 PTZ00121
MAEBL; Provisional
139-426 8.23e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  139 EVRRLREARKSQLHREQQLQARGRALEEERA-GLEQRLREQQAAQERCQRLREDWEAGslELLRLKDENYMIAMRLAQLS 217
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAA 1506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  218 EEKNSAvlrsRDLQLAVDQLKLKVSRLEEEcallRRGRGPPPGAEEKEKEpdgvdllSELR-AENQRLTASLQELQEGLQ 296
Cdd:PTZ00121 1507 EAKKKA----DEAKKAEEAKKADEAKKAEE----AKKADEAKKAEEKKKA-------DELKkAEELKKAEEKKKAEEAKK 1571
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  297 QEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQwAEELRDKylqemEDLRLKHRTLLKDCDLYKHRMA 376
Cdd:PTZ00121 1572 AEEDKNMALRKAEEA--------KKAEEARIEEVMKLYEEEKKMK-AEEAKKA-----EEAKIKAEELKKAEEEKKKVEQ 1637
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194474088  377 TVLAQLEEIEK-ERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDE 426
Cdd:PTZ00121 1638 LKKKEAEEKKKaEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
141-428 1.27e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  141 RRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREdweagslELLRLKDENYMIAMRLAQLSEEK 220
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKepdgvdlLSELRAENQRLTASLQELQEGLQQEMS 300
Cdd:COG4372   139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-------LDELLKEANRNAEKEEELAEAEKLIES 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  301 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 380
Cdd:COG4372   212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 194474088  381 QLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELL 428
Cdd:COG4372   292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
107-446 2.07e-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: 42.26  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   107 HFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQ-----------------ARGRALEEERA 169
Cdd:TIGR00618  425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqihlqetrkkavvlARLLELQEEPC 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   170 GLEQRLREQQAA----------QERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKL 239
Cdd:TIGR00618  505 PLCGSCIHPNPArqdidnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   240 KVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSEL--RAENQRLTASLQELQEGLQQEMsrpgaAGSERILLDILEH 317
Cdd:TIGR00618  585 DIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKLqpEQDLQDVRLHLQQCSQELALKL-----TALHALQLTLTQE 658
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   318 DWREA-QDSRQELCQKLHAVQGELQ-----------WAEEL--RDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQ-- 381
Cdd:TIGR00618  659 RVREHaLSIRVLPKELLASRQLALQkmqsekeqltyWKEMLaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAre 738
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474088   382 ------LEEIEKERDQAIQSRDRIQLQYSQSLI----EKDQYRKQVRGLEAERDELLTTVTSLegtkAMLEAQLQ 446
Cdd:TIGR00618  739 dalnqsLKELMHQARTVLKARTEAHFNNNEEVTaalqTGAELSHLAAEIQFFNRLREEDTHLL----KTLEAEIG 809
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
138-442 2.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  138 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLR-------------EDWEAGSLELLRLKD 204
Cdd:PRK03918  293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklkelekrleelEERHELYEEAKAKKE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  205 ENYMIAMRLAQLSEEKNSAVL-----RSRDLQLAVDQLKLKVSRLEEECALLR---------RGRGPPPGAE--EKEKEp 268
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELeelekAKEEIEEEISKITARIGELKKEIKELKkaieelkkaKGKCPVCGREltEEHRK- 451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  269 dgvDLLSELRAENQRLTASLQELQEGLQQ----------EMSRPGAAGSERILLDI---------------LEHDWREAq 323
Cdd:PRK03918  452 ---ELLEEYTAELKRIEKELKEIEEKERKlrkelrelekVLKKESELIKLKELAEQlkeleeklkkynleeLEKKAEEY- 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  324 dsrQELCQKLHAVQGELQWAEelrdKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEI----EKERDQAIQSRDRI 399
Cdd:PRK03918  528 ---EKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPF 600
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 194474088  400 QLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLE 442
Cdd:PRK03918  601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
139-388 3.40e-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: 41.58  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIamrLAQLSE 218
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE---RASLEE 887
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLqqe 298
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELR-------------------EKLAQLELRLEGLEVRIDNLQERL--- 945
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   299 msrpgaAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLK-DCDLYKHRmAT 377
Cdd:TIGR02168  946 ------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAqKEDLTEAK-ET 1018
                          250
                   ....*....|.
gi 194474088   378 VLAQLEEIEKE 388
Cdd:TIGR02168 1019 LEEAIEEIDRE 1029
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
136-456 5.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  136 LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrLAQ 215
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------LES 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  216 LSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaEEKEKEpdgvdlLSELRAENQRLTASLQELQEGL 295
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------AEREEE------LKELEEQLESLQEELAALEQEL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  296 QQEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDcdlykhrM 375
Cdd:COG4372   174 QALSEAEAEQALDELL--------KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA-------L 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  376 ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQGGSSLK 455
Cdd:COG4372   239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318

                  .
gi 194474088  456 A 456
Cdd:COG4372   319 A 319
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
29-101 6.44e-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: 36.80  E-value: 6.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194474088    29 ERIEGVRHRLTRALNPAKLTPYLRQCrvLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRG-FEAFLEALE 101
Cdd:pfam16739    7 RLLRLFRPRLKDTIKPTEILPHLPEC--LTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGwFRAFLDALR 78
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
272-449 6.61e-03

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: 40.13  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  272 DLLSELRAENQRLTASLQELQEgLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELqwAEELRDKYL 351
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRA-LEQE-------------LAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  352 QEMEDlRLKH-------RTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:COG4942   116 LGRQP-PLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
                         170       180
                  ....*....|....*....|....*
gi 194474088  425 DELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQ 219
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
149-449 8.05e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   149 SQLHREQQL-----------QARGRALEEERAGLEQRLREQQAAQERCQRL-------------REDWEAGSLELL---- 200
Cdd:pfam01576  468 SQLQDTQELlqeetrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlqaqlsdmkkKLEEDAGTLEALeegk 547
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   201 -RLKDEnymiAMRLAQLSEEKNSAV-----LRSR------DLQLAVDQLKLKVSRLE-----------EECALL-----R 252
Cdd:pfam01576  548 kRLQRE----LEALTQQLEEKAAAYdklekTKNRlqqeldDLLVDLDHQRQLVSNLEkkqkkfdqmlaEEKAISaryaeE 623
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   253 RGRGPppgAEEKEKEPDGVDLLSELRaENQRLTASLQELQEGLQQEM----SRPGAAGSErilLDILEHDWREAQDSRQE 328
Cdd:pfam01576  624 RDRAE---AEAREKETRALSLARALE-EALEAKEELERTNKQLRAEMedlvSSKDDVGKN---VHELERSKRALEQQVEE 696
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   329 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH-RTLLKDCDLYKHRMATVLAQLEEIE-------KERDQAIQSRDRIQ 400
Cdd:pfam01576  697 MKTQLEELEDELQATEDAKLRLEVNMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEaelederKQRAQAVAAKKKLE 776
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088   401 LQYS--QSLIE-----KDQYRKQVRGLEAE--------------RDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:pfam01576  777 LDLKelEAQIDaankgREEAVKQLKKLQAQmkdlqreleearasRDEILAQSKESEKKLKNLEAELLQLQ 846
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
212-447 8.07e-03

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: 39.75  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  212 RLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgaeekekepdgvdlLSELRAENQRLTASLQEL 291
Cdd:COG4942    42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-------------------LAELEKEIAELRAELEAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  292 QEGLQQ---EMSRPGAAGSERILLdilehdwreAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLkdc 368
Cdd:COG4942   103 KEELAEllrALYRLGRQPPLALLL---------SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474088  369 dlykhrmatvlAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 447
Cdd:COG4942   171 -----------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
127-219 8.12e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  127 EGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLRE----QQAAQERCQRLREDWEAGSLE-LLR 201
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEleekQQELEAQLEQLQEKAAETSQErKQK 217
                          90
                  ....*....|....*...
gi 194474088  202 LKDENYMIAMRLaQLSEE 219
Cdd:PRK11448  218 RKEITDQAAKRL-ELSEE 234
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
153-393 9.25e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  153 REQQLQARGRALEEERAGLEQRLREqqaAQERCQRLREDweagsLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQL 232
Cdd:COG3206   169 RREEARKALEFLEEQLPELRKELEE---AEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  233 AVDQLKlkvSRLEEECALLRRGRGPPPGAEEKEKEpdgVDLLSELRAENQRLT----------ASLQELQEGLQQEMSRp 302
Cdd:COG3206   241 RLAALR---AQLGSGPDALPELLQSPVIQQLRAQL---AELEAELAELSARYTpnhpdvialrAQIAALRAQLQQEAQR- 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474088  303 gaagseriLLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLlkdcdlykhrmATVLAQL 382
Cdd:COG3206   314 --------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-----------ESLLQRL 374
                         250
                  ....*....|.
gi 194474088  383 EEIEKERDQAI 393
Cdd:COG3206   375 EEARLAEALTV 385
 
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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