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Conserved domains on  [gi|1958789716|ref|XP_038935186|]
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caspase recruitment domain-containing protein 10 isoform X2 [Rattus norvegicus]

Protein Classification

FYN-binding protein 1; SH3 domain-containing protein( domain architecture ID 12962297)

FYN-binding protein 1 acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells; 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 ...
76-161 8.51e-54

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: 182.03  E-value: 8.51e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807      1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08807     81 HFTLLT 86
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-499 1.23e-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: 78.83  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196    223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196    303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196    370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789716  428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
784-849 6.45e-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: 41.99  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  784 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 849
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 ...
76-161 8.51e-54

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: 182.03  E-value: 8.51e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807      1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08807     81 HFTLLT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
77-163 4.56e-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: 74.13  E-value: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   77 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1958789716  156 HFTLLTGQ 163
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-499 1.23e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196    223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196    303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196    370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789716  428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
193-499 1.71e-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: 68.93  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  193 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 272
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  273 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 352
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  353 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 432
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  433 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
mukB PRK04863
chromosome partition protein MukB;
204-484 6.22e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.73  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  204 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdwEAGSLELLrlkDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 281
Cdd:PRK04863   844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR--LLPRLNLL---ADETLAD-RVEEIREQLDEAEEAKRFVQQh 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  282 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 350
Cdd:PRK04863   917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  351 pgaAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 430
Cdd:PRK04863   997 ---AEQER---TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958789716  431 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
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 ...
202-502 1.87e-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: 49.02  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  202 REQQLQARGRALEEERAGLEQRLREQQAAQERCQ--RLREDWEAGSLE--LLRLKDENY-------MIAMRLAQLS---- 266
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQleKVTTEAKIKKLEedILLLEDQNSklskerkLLEERISEFTsnla 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  267 --EEKNSAVLRSRDLQLAV-----DQLKlKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSELRAENQRLTASLQE 339
Cdd:pfam01576  170 eeEEKAKSLSKLKNKHEAMisdleERLK-KEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  340 LQEGLQQEMSRPGAAGS-----ERILLDILEHDWRE------AQDSRQELCQKLHAVQGELQ-------WAEELRDKYLQ 401
Cdd:pfam01576  248 ALARLEEETAQKNNALKkirelEAQISELQEDLESEraarnkAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQ 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  402 EMEDLRlkhRTLLKDCDLYKhrmatvlAQLEEIEKERDQAIqsrDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVT 481
Cdd:pfam01576  328 EVTELK---KALEEETRSHE-------AQLQEMRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
                          330       340
                   ....*....|....*....|....*...
gi 1958789716  482 SLEGTKA-------MLEAQLQRTQGGSS 502
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 ...
784-849 6.45e-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: 41.99  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  784 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 849
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 ...
76-161 8.51e-54

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: 182.03  E-value: 8.51e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08807      1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08807     81 HFTLLT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
76-161 3.66e-40

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: 142.90  E-value: 3.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPcrANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08785      1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08785     79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
76-161 6.51e-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: 130.90  E-value: 6.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08808      1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08808     81 LYKLVT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
76-161 2.88e-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: 97.64  E-value: 2.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   76 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:cd08806      1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                   ....*.
gi 1958789716  156 HFTLLT 161
Cdd:cd08806     81 LYTQVT 86
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
77-161 3.88e-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: 97.30  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   77 WERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 156
Cdd:cd08809      2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81

                   ....*
gi 1958789716  157 FTLLT 161
Cdd:cd08809     82 YKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
77-163 4.56e-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: 74.13  E-value: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   77 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 155
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1958789716  156 HFTLLTGQ 163
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-499 1.23e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196    223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 347
Cdd:COG1196    303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  348 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 427
Cdd:COG1196    370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789716  428 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
84-156 5.04e-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: 62.53  E-value: 5.04e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789716   84 RHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 156
Cdd:cd01671      5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE---KTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPH 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
193-499 1.71e-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: 68.93  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  193 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 272
Cdd:TIGR02168  666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  273 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 352
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  353 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 432
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  433 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
163-498 3.69e-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: 67.79  E-value: 3.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  163 QEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQrlrEQQAAQERCQRLREDWE 242
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ---EEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  243 AGSLELLRLKDENYMIAMRLAQLSEEKNsavlrsrdlqlavdQLKLKVSRLEEEcallrrgrgpppgaEEKEKEPDGVDL 322
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLH--------------KLEEALNDLEAR--------------LSHSRIPEIQAE 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  323 LSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE 402
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  403 MEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLttvtS 482
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL----S 952
                          330
                   ....*....|....*.
gi 1958789716  483 LEGTKAMLEAQLQRTQ 498
Cdd:TIGR02169  953 LEDVQAELQRVEEEIR 968
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
78-150 1.32e-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: 55.82  E-value: 1.32e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789716   78 ERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALE 150
Cdd:cd08810      3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR---TTRKKRVDKLLDILAREGPDGLDALIESIR 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
190-484 1.54e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  190 RRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 269
Cdd:COG1196    262 LAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  270 NSAVLRSRDLQLAVDQLKLKVSRLEEEcaLLRrgrgpppgAEEKEKEpdgvdLLSELRAENQRLTASLQELQEGLQQEMS 349
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEA--LLE--------AEAELAE-----AEEELEELAEELLEALRAAAELAAQLEE 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  350 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 429
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958789716  430 QLEEiEKERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDELLTTVTSLE 484
Cdd:COG1196    485 ELAE-AAARLLLLLEAEADYEGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYE 537
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
222-498 2.36e-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: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  222 QRLREQQAAQERCQRLREDWEAGSLELLRLKDENymIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallr 301
Cdd:COG1196    203 EPLERQAEKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLE----- 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  302 rgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWRE----AQDSRQE 377
Cdd:COG1196    276 --------LEELELE------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEELEE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  378 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLI 457
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958789716  458 EKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:COG1196    422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
173-486 1.34e-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: 56.22  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  173 LDEEGPEGLTQF--LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRL-----------REQQAAQERCQRLRE 239
Cdd:TIGR02168  717 LRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeeelaeaeAEIEELEAQIEQLKE 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  240 DWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGppPGAEEKEKEPDG 319
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--ELEELIEELESE 874
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  320 VDLLSELRAENQRLTASLQELQEGLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDkY 399
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEE-------------LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-N 940
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  400 LQEMedLRLKHRTLLKDcdlykhrmatVLAQLEEIEKERDQAIQSRDRIQLQYSQ-------SLIEKDQYRKQVRGLEAE 472
Cdd:TIGR02168  941 LQER--LSEEYSLTLEE----------AEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
                          330
                   ....*....|....
gi 1958789716  473 RDELLTTVTSLEGT 486
Cdd:TIGR02168 1009 KEDLTEAKETLEEA 1022
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
191-499 1.77e-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: 55.83  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  191 RLREARKsQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELL-----RLKDENYMIAMRLAQL 265
Cdd:TIGR02168  173 RRKETER-KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEA 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  266 SEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 345
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEE-------------IEELQKE------LYALANEISRLEQQKQILRERLA 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  346 QeMSRPGAAGSERIL-----LDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLY 420
Cdd:TIGR02168  313 N-LERQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789716  421 KHRMATVLAQLEEIEKERDQAIQSRDRiqLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
189-454 2.42e-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: 51.88  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  189 VRRLREARK----SQLH------REQQLQARGRALEEERAGLEQRLREQQAAQERCQRL------------RED-WEAGS 245
Cdd:COG3096    419 VQALEKARAlcglPDLTpenaedYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQaWQTAR 498
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  246 lELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKlkvsrleeecALLRRGRGPPPGAEEKEkepdgvDLLSE 325
Cdd:COG3096    499 -ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----------EFCQRIGQQLDAAEELE------ELLAE 561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  326 LRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQklhavqgelQWAEELRDkyLQEMED 405
Cdd:COG3096    562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE---------QSGEALAD--SQEVTA 630
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958789716  406 LrlkhrtllkdcdlykhrMATVLAQLEEIEKERDQAIQSRDRIQLQYSQ 454
Cdd:COG3096    631 A-----------------MQQLLEREREATVERDELAARKQALESQIER 662
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-476 2.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  187 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEA-----------GSLELLRLKDEN 255
Cdd:COG1196    456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalllaglrglaGAVAVLIGVEAA 535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  256 YMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLK-LKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAENQRLT 334
Cdd:COG1196    536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  335 ASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQD-----------SRQELCQKLHAVQGELQWAEELRDKYLQEM 403
Cdd:COG1196    616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggSRRELLAALLEAEAELEELAERLAEEELEL 695
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  404 EDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEK-----------DQYRKQVRGLEAE 472
Cdd:COG1196    696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELERLERE 775

                   ....
gi 1958789716  473 RDEL 476
Cdd:COG1196    776 IEAL 779
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
211-484 3.72e-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: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  211 RALEEERAGLEQRLrEQQAAQERCQRLREDWEAGSLELLR--------LKDENymIAMRLAQLSEEKNSAvlrsRDLQLA 282
Cdd:COG3096    839 AALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADET--LADRLEELREELDAA----QEAQAF 911
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  283 VDQLKLKVSRLEEECALLRRgrgpPPGAEEkekepdgvdllsELRAENQRLTASLQELQEG---LQQEMSR--------- 350
Cdd:COG3096    912 IQQHGKALAQLEPLVAVLQS----DPEQFE------------QLQADYLQAKEQQRRLKQQifaLSEVVQRrphfsyeda 975
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  351 PGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELqwaeelrDKYLQEMEDLRLKHRTllkdcdlyKHRMATVLAQ 430
Cdd:COG3096    976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLASLKSSRDA--------KQQTLQELEQ 1040
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  431 -LEEIEKERD-----QAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
Cdd:COG3096   1041 eLEELGVQADaeaeeRARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
211-496 4.00e-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: 51.22  E-value: 4.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  211 RALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDenymiamRLAQLSEEKNSAvLRSRDLQLAVDQLKLKV 290
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRREREKA-ERYQALLKEKREYEGYE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  291 SRLEEEcallrrgrgpppgAEEKEKEpdgvdllsELRAENQRLTASLQELQEGLQQEMSRPGAAgsERILLDILEHDWRE 370
Cdd:TIGR02169  228 LLKEKE-------------ALERQKE--------AIERQLASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDL 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  371 AQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQ---AIQSRD- 446
Cdd:TIGR02169  285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKe 364
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  447 -----RIQLQ-----YSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 496
Cdd:TIGR02169  365 eledlRAELEevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-350 4.53e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  190 RRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQERCQRLRE------DWEAGSLELLRLKDE-------NY 256
Cdd:COG4913    609 RAKLAALEAEL---AELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAElerldasSD 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  257 MIA---MRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAEN--Q 331
Cdd:COG4913    686 DLAaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAveR 765
                          170
                   ....*....|....*....
gi 1958789716  332 RLTASLQELQEGLQQEMSR 350
Cdd:COG4913    766 ELRENLEERIDALRARLNR 784
mukB PRK04863
chromosome partition protein MukB;
204-484 6.22e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.73  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  204 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdwEAGSLELLrlkDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 281
Cdd:PRK04863   844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR--LLPRLNLL---ADETLAD-RVEEIREQLDEAEEAKRFVQQh 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  282 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 350
Cdd:PRK04863   917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  351 pgaAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 430
Cdd:PRK04863   997 ---AEQER---TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958789716  431 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 484
Cdd:PRK04863  1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-499 6.94e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  194 EARKSQLHRE-QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrlaqlseeknsa 272
Cdd:TIGR02168  273 RLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE------------------ 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  273 vlrsrdLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLQQEMSRpg 352
Cdd:TIGR02168  335 ------LAEELAELEEKLEELKEELESLE-------------------AELEELEAELEELESRLEELEEQLETLRSK-- 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  353 aagserilLDILEHDWREAQDSRQELCQKLHAVQGElqwaeelRDKYLQEMEDLRLKhrtllkdcdLYKHRMATVLAQLE 432
Cdd:TIGR02168  388 --------VAQLELQIASLNNEIERLEARLERLEDR-------RERLQQEIEELLKK---------LEEAELKELQAELE 443
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  433 EIEKERDQAIQSRDRIQLQYSQSliekdqyRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 499
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEEL-------REELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
190-502 1.44e-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: 49.30  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  190 RRLREARKSQLHREQQlqargrALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymIAMRLAQLSEEk 269
Cdd:TIGR02169  218 KEKREYEGYELLKEKE------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE---LNKKIKDLGEE- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  270 nsavlRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEms 349
Cdd:TIGR02169  288 -----EQLRVKEKIGELEAEIASLERSIAEKERE------LEDAEER------LAKLEAEIDKLLAEIEELEREIEEE-- 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  350 rpgaagseRILLDILEHDWREAQDSRQELCQKLHAVQGELQ-WAEELR------DKYLQEMEDL-----RLKHRTLLKDC 417
Cdd:TIGR02169  349 --------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKdyreklEKLKREINELkreldRLQEELQRLSE 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  418 DLYKHRM--ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQ 495
Cdd:TIGR02169  421 ELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
                          330
                   ....*....|
gi 1958789716  496 ---RTQGGSS 502
Cdd:TIGR02169  501 aseERVRGGR 510
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
202-502 1.87e-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: 49.02  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  202 REQQLQARGRALEEERAGLEQRLREQQAAQERCQ--RLREDWEAGSLE--LLRLKDENY-------MIAMRLAQLS---- 266
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQleKVTTEAKIKKLEedILLLEDQNSklskerkLLEERISEFTsnla 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  267 --EEKNSAVLRSRDLQLAV-----DQLKlKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSELRAENQRLTASLQE 339
Cdd:pfam01576  170 eeEEKAKSLSKLKNKHEAMisdleERLK-KEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  340 LQEGLQQEMSRPGAAGS-----ERILLDILEHDWRE------AQDSRQELCQKLHAVQGELQ-------WAEELRDKYLQ 401
Cdd:pfam01576  248 ALARLEEETAQKNNALKkirelEAQISELQEDLESEraarnkAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQ 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  402 EMEDLRlkhRTLLKDCDLYKhrmatvlAQLEEIEKERDQAIqsrDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVT 481
Cdd:pfam01576  328 EVTELK---KALEEETRSHE-------AQLQEMRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
                          330       340
                   ....*....|....*....|....*...
gi 1958789716  482 SLEGTKA-------MLEAQLQRTQGGSS 502
Cdd:pfam01576  395 TLQQAKQdsehkrkKLEGQLQELQARLS 422
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
186-411 1.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  186 MTEVRRLREARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQERCQRlredweagSLELLRLKDENYMIAMRLAQL 265
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE--------ELEKLEKLLQLLPLYQELEAL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  266 SEEknsavlrsrdlqlavdqLKLKVSRLEEecallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 345
Cdd:COG4717    138 EAE-----------------LAELPERLEE--------------LEERLEE------LRELEEELEELEAELAELQEELE 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958789716  346 QEMSRPGAAGSERiLLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHR 411
Cdd:COG4717    181 ELLEQLSLATEEE-LQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-407 2.01e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  187 TEVRRLREARKSQLHRE--QQLQARGRALEEERAGLEQRLREQQA----AQERCQRLREDWEAGSLEllrlkdenymiam 260
Cdd:COG4913    272 AELEYLRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEArldaLREELDELEAQIRGNGGD------------- 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  261 RLAQLSEEKnsavlrsRDLQLAVDQLKLKVSRLEEECALLrrGRGPPPGAEEkekepdgvdlLSELRAENQRLTASLQEL 340
Cdd:COG4913    339 RLEQLEREI-------ERLERELEERERRRARLEALLAAL--GLPLPASAEE----------FAALRAEAAALLEALEEE 399
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  341 QEGLQQEMsrpgaagserilldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 407
Cdd:COG4913    400 LEALEEAL--------------------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
mukB PRK04863
chromosome partition protein MukB;
192-294 2.33e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.80  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  192 LREARkSQLHREQQLQARGRALEEeragLEQRLREQQAAQER----CQRLREDWEAGS-LELLRLKDEnymiaMRLAQLS 266
Cdd:PRK04863   502 LRRLR-EQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLlaefCKRLGKNLDDEDeLEQLQEELE-----ARLESLS 571
                           90       100
                   ....*....|....*....|....*...
gi 1958789716  267 EEKNSAVLRSRDLQLAVDQLKLKVSRLE 294
Cdd:PRK04863   572 ESVSEARERRMALRQQLEQLQARIQRLA 599
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
188-491 2.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSL-ELLRLKDENYMIAMRLAQLS 266
Cdd:COG4717    133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELE 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  267 EEKNSAVLRSRDLQLAVDQLKLKVSRLEEE----------------CALLRRGRGPPPGAEE------------------ 312
Cdd:COG4717    213 EELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalLALLGLGGSLLSLILTiagvlflvlgllallfll 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  313 -KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQW 391
Cdd:COG4717    293 lAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  392 AEELRDKYLQEMEDLRLKHRTLLKDCDLyKHRMATVLAQLEEIEKERDQAIQSRDRIQLQysqslIEKDQYRKQVRGLEA 471
Cdd:COG4717    373 AALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEE 446
                          330       340
                   ....*....|....*....|
gi 1958789716  472 ERDELLTTVTSLEGTKAMLE 491
Cdd:COG4717    447 ELEELREELAELEAELEQLE 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
179-347 2.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  179 EGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMI 258
Cdd:COG1196    319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  259 AMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRgrgpppgAEEKEKEpdgvdLLSELRAENQRLTASLQ 338
Cdd:COG1196    399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAE-----EEAELEEEEEALLELLA 466

                   ....*....
gi 1958789716  339 ELQEGLQQE 347
Cdd:COG1196    467 ELLEEAALL 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-498 3.09e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRR-----------------------------------GRGPPPGAEE 312
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaarllllleaeadyegflegvkaalllaglRGLAGAVAVL 529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  313 --KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQ 390
Cdd:COG1196    530 igVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  391 WAEELRDKYLQEMEDLRLKHRTLlkdcDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLE 470
Cdd:COG1196    610 EADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
                          330       340
                   ....*....|....*....|....*...
gi 1958789716  471 AERDELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:COG1196    686 ERLAEEELELEEALLAEEEEERELAEAE 713
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
169-476 3.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  169 CSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGlEQRLREQQAAQERCQRLREDWEAGSLEL 248
Cdd:PRK03918   441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEE 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  249 LRLKDENYmiamrlaqlseEKnsavLRSRDLQLAVDQLKLKvSRLEEECALLRRGRGPPPGAEEKEKEPDgvDLLSELRA 328
Cdd:PRK03918   520 LEKKAEEY-----------EK----LKEKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELA--ELLKELEE 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  329 EN----QRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE-M 403
Cdd:PRK03918   582 LGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeY 661
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789716  404 EDLRLKHRTLLKdcdlykhRMATVLAQLEEIEKERDQAIQSRDRIQLQysqsLIEKDQYRKQVRGLEAERDEL 476
Cdd:PRK03918   662 EELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERV 723
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
164-491 3.58e-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: 48.04  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  164 EPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEEraglEQRLREQQAAQERC-QRLREDWE 242
Cdd:TIGR00618  512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCdNRSKEDIP 587
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  243 AGSLELLRLKDENYMIAMRLAQLSEEkNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDL 322
Cdd:TIGR00618  588 NLQNITVRLQDLTEKLSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  323 LSELRAEN-QRLTASLQELQEGLQQEMS-RPGAAGSERILLDILEH---DWREaqdsRQELCQKLHAVQGELQWAEELRD 397
Cdd:TIGR00618  667 IRVLPKELlASRQLALQKMQSEKEQLTYwKEMLAQCQTLLRELETHieeYDRE----FNEIENASSSLGSDLAAREDALN 742
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  398 KYLQEMEDLR---LKHRTLLKDCDLYKHRMA-TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 473
Cdd:TIGR00618  743 QSLKELMHQArtvLKARTEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
                          330
                   ....*....|....*...
gi 1958789716  474 DELLttVTSLEGTKAMLE 491
Cdd:TIGR00618  823 CETL--VQEEEQFLSRLE 838
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
188-366 4.86e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENymiamRLAQLSE 267
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-----RFAAALG 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRsRDLQLAVDQLKLKVSRLEEECALLRRG---RGPPPGAE---EKEKEPDGVDLLSELRAEN---------QR 332
Cdd:COG4913    761 DAVERELR-ENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADldaDLESLPEYLALLDRLEEDGlpeyeerfkEL 839
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958789716  333 LTASLQELQEGLQQEMSRPGAAGSERI--LLDILEH 366
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 ...
784-849 6.45e-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: 41.99  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789716  784 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 849
Cdd:cd12026      1 DSFYIRTHFEY-EKESPYGLSFNKGEVFRVVDTLYNgKLGSWLAIRIGK-NHKEVERGIIPNKNRAE 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
188-498 8.00e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 8.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAgSLELLRLKDENYMIAMRLAQLSE 267
Cdd:COG4717     75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEELEE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EknsaVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgppPGAEEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQQ- 346
Cdd:COG4717    154 R----LEELRELEEELEELEAELAELQEELEELLEQ----LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEl 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  347 -------EMSRPGAAGSERI-----------LLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRL 408
Cdd:COG4717    226 eeeleqlENELEAAALEERLkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  409 KHRTLLKDCDLYKHRMATVLAQLE-EIEKERDQAIQSRDRI-QLQYSQSLIEKDQYRKQVRGLEAERDELLTT--VTSLE 484
Cdd:COG4717    306 ELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEagVEDEE 385
                          330
                   ....*....|....
gi 1958789716  485 GTKAMLEAQLQRTQ 498
Cdd:COG4717    386 ELRAALEQAEEYQE 399
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
787-849 8.60e-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: 8.60e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789716  787 YIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 849
Cdd:cd11859      1 YIRTHFDY-EKPAKGELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-423 9.41e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 9.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  170 SMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLqargRALEEERAGLE--QRLREQQAAQERCQRLREDWEAgSLE 247
Cdd:COG4913    215 EYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAEryAAARERLAELEYLRAALRLWFA-QRR 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  248 LLRLKDEnymiamrLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallRRGrgpppgaeekekepDGVDLLSELR 327
Cdd:COG4913    290 LELLEAE-------LEELRAELARLEAELERLEARLDALREELDELEAQ----IRG--------------NGGDRLEQLE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  328 AENQRLTASLQELQEGLQQEMSRPGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 407
Cdd:COG4913    345 REIERLERELEERERRRARLEALLAALGLP------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
                          250
                   ....*....|....*.
gi 1958789716  408 LKHRTLLKDCDLYKHR 423
Cdd:COG4913    419 RELRELEAEIASLERR 434
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
186-493 1.11e-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: 46.65  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  186 MTEVRRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRlaql 265
Cdd:pfam15921  333 LREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR---- 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  266 sEEKNSAVLRSrdLQLAVDQLKLKVSRLEeecALLRRGRGPPPGAEEKEkepdgvdlLSELRAENQ------RLTASLQE 339
Cdd:pfam15921  407 -DTGNSITIDH--LRRELDDRNMEVQRLE---ALLKAMKSECQGQMERQ--------MAAIQGKNEslekvsSLTAQLES 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  340 LQEGLQQEMSRPGAagsERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH---RTLLKD 416
Cdd:pfam15921  473 TKEMLRKVVEELTA---KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTE 549
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  417 CDLYKHRMA-------TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAM 489
Cdd:pfam15921  550 CEALKLQMAekdkvieILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629

                   ....
gi 1958789716  490 LEAQ 493
Cdd:pfam15921  630 LELE 633
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
190-524 1.33e-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: 46.12  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  190 RRLREARKSQLHREQQLQARGRALEEERAgLEQRLREQQAAQERcqrlREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 269
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRARIEELRA-QEAVLEETQERINR----ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  270 NS-AVLRSRDLQLAVDQLKLKVSR-----LEEECALLRRGRGPPPG-AEEKEKEpdgVDLLSELRAENQRLTASLQELQe 342
Cdd:TIGR00618  321 RSrAKLLMKRAAHVKQQSSIEEQRrllqtLHSQEIHIRDAHEVATSiREISCQQ---HTLTQHIHTLQQQKTTLTQKLQ- 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  343 glqqemsrpgAAGSERILLDILEHDwREAQDSRQE-LCQKLHAVQGElqwaEELRDKYLQEMEDLRLKHRTLLKDCDLYK 421
Cdd:TIGR00618  397 ----------SLCKELDILQREQAT-IDTRTSAFRdLQGQLAHAKKQ----QELQQRYAELCAAAITCTAQCEKLEKIHL 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  422 HRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR-TQGG 500
Cdd:TIGR00618  462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLE 541
                          330       340
                   ....*....|....*....|....
gi 1958789716  501 SSLKacASSHSLCSNLSSTWSLSE 524
Cdd:TIGR00618  542 TSEE--DVYHQLTSERKQRASLKE 563
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-498 1.50e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  191 RLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK- 269
Cdd:COG4717    115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEl 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  270 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVD-LLSELRAENQRLTASLQELQEGLQQEM 348
Cdd:COG4717    195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKeARLLLLIAAALLALLGLGGSLLSLILT 274
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  349 SRPGAAGSERILLDILEHDWREAQDSRQELcQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVL 428
Cdd:COG4717    275 IAGVLFLVLGLLALLFLLLAREKASLGKEA-EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  429 AQLEEIEKERDQAIQSRDRIQL----------QYSQSLIEKDQY---RKQVRGLEAERDELLTTVTSL--EGTKAMLEAQ 493
Cdd:COG4717    354 REAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYqelKEELEELEEQLEELLGELEELleALDEEELEEE 433

                   ....*
gi 1958789716  494 LQRTQ 498
Cdd:COG4717    434 LEELE 438
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
320-476 1.62e-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: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  320 VDLLSELRAENQRLTASLQELQEgLQQEMSRPGAAGSERIL------LDILEHDWREAQDSRQELCQKLHAVQGELqwaE 393
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQRRLelleaeLEELRAELARLEAELERLEARLDALREEL---D 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  394 ELRDKYLQ-----------EMEDLRLKHRTLLKDCDLYKHRMATV-----------LAQLEEIEKERDQAIQSRDRIQLQ 451
Cdd:COG4913    327 ELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEA 406
                          170       180
                   ....*....|....*....|....*
gi 1958789716  452 YSQSLIEKDQYRKQVRGLEAERDEL 476
Cdd:COG4913    407 LAEAEAALRDLRRELRELEAEIASL 431
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
290-473 2.19e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  290 VSRLEEECALLRRGRGPPP-----GAEEKEKEpdgVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDIL 364
Cdd:COG4717     48 LERLEKEADELFKPQGRKPelnlkELKELEEE---LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  365 E------HDWREAQDSRQELCQKLHAVQGELQWAEELRDKY---LQEMEDLRLKHRTLLKDCDLYKH-RMATVLAQLEEI 434
Cdd:COG4717    125 LqllplyQELEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEeELQDLAEELEEL 204
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958789716  435 EKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 473
Cdd:COG4717    205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
310-461 3.20e-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: 42.97  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  310 AEEKEKEPDGVDLLSELRAENQRLTASLQELQ---EGLQQEMsrpgaAGSER---IL------LDILEHDWREAQDSRQE 377
Cdd:pfam13851   36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQeevEELRKQL-----ENYEKdkqSLknlkarLKVLEKELKDLKWEHEV 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  378 LCQKLHAVQGELQwaeELRDKYLQEMEDLRLKhrTLLKDCdLYKHRMATVLAQLEEIEKERDQAIQS-------RDRIQL 450
Cdd:pfam13851  111 LEQRFEKVERERD---ELYDKFEAAIQDVQQK--TGLKNL-LLEKKLQALGETLEKKEAQLNEVLAAanldpdaLQAVTE 184
                          170
                   ....*....|.
gi 1958789716  451 QYSQSLIEKDQ 461
Cdd:pfam13851  185 KLEDVLESKNQ 195
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
376-494 3.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  376 QELCQKLHAVQGELQWAEELRDKylQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQS 455
Cdd:COG4913    258 RELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958789716  456 -LIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQL 494
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 ...
786-849 4.42e-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: 4.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958789716  786 FYIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 849
Cdd:cd12028      3 FYIRTHFDY-EPDPPSGLSFTRGEVFHVLDTMHRGKlGSWLAVRMGR-DLREMEKGIIPNQSRAE 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-442 4.87e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAA----QERCQRLREDWEAGSLELLRLKDENYMIAMRLA 263
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  264 QLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALL--RRGRgpppgaEEKEKEPDGVDLLSELRAENQRLTASLQELQ 341
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedRRER------LQQEIEELLKKLEEAELKELQAELEELEEEL 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  342 EGLQQEMSRPGAAgserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR--LKHRTLLKDcdl 419
Cdd:TIGR02168  450 EELQEELERLEEA------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSG--- 520
                          250       260
                   ....*....|....*....|...
gi 1958789716  420 ykhrMATVLAQLEEIEKERDQAI 442
Cdd:TIGR02168  521 ----ILGVLSELISVDEGYEAAI 539
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
190-477 6.50e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 6.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  190 RRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREdweagslELLRLKDENYMIAMRLAQLSEEK 269
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQI 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  270 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKepdgvdlLSELRAENQRLTASLQELQEGLQQEMS 349
Cdd:COG4372    139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-------LDELLKEANRNAEKEEELAEAEKLIES 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  350 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 429
Cdd:COG4372    212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1958789716  430 QLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELL 477
Cdd:COG4372    292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
PTZ00121 PTZ00121
MAEBL; Provisional
188-475 6.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERA-GLEQRLREQQAAQERCQRLREDWEAGslELLRLKDENYMIAMRLAQLS 266
Cdd:PTZ00121  1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAA 1506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  267 EEKNSAvlrsRDLQLAVDQLKLKVSRLEEEcallRRGRGPPPGAEEKEKEpdgvdllSELR-AENQRLTASLQELQEGLQ 345
Cdd:PTZ00121  1507 EAKKKA----DEAKKAEEAKKADEAKKAEE----AKKADEAKKAEEKKKA-------DELKkAEELKKAEEKKKAEEAKK 1571
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  346 QEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQwAEELRDKylqemEDLRLKHRTLLKDCDLYKHRMA 425
Cdd:PTZ00121  1572 AEEDKNMALRKAEEA--------KKAEEARIEEVMKLYEEEKKMK-AEEAKKA-----EEAKIKAEELKKAEEEKKKVEQ 1637
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958789716  426 TVLAQLEEIEK-ERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDE 475
Cdd:PTZ00121  1638 LKKKEAEEKKKaEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
156-495 8.66e-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: 43.42  E-value: 8.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  156 HFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQ---------ARGRALEEERAgleQRLRE 226
Cdd:TIGR00618  425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqihlqeTRKKAVVLARL---LELQE 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  227 QQ---------------------AAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQ 285
Cdd:TIGR00618  502 EPcplcgscihpnparqdidnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  286 LKLKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSEL--RAENQRLTASLQELQEGLQQEMsrpgaAGSERILLDI 363
Cdd:TIGR00618  582 SKEDIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKLqpEQDLQDVRLHLQQCSQELALKL-----TALHALQLTL 655
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  364 LEHDWREA-QDSRQELCQKLHAVQGELQ-----------WAEEL--RDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 429
Cdd:TIGR00618  656 TQERVREHaLSIRVLPKELLASRQLALQkmqsekeqltyWKEMLaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLA 735
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789716  430 Q--------LEEIEKERDQAIQSRDRIQLQYSQSLI----EKDQYRKQVRGLEAERDELLTTVTSLegtkAMLEAQLQ 495
Cdd:TIGR00618  736 AredalnqsLKELMHQARTVLKARTEAHFNNNEEVTaalqTGAELSHLAAEIQFFNRLREEDTHLL----KTLEAEIG 809
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
187-491 1.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  187 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLR-------------EDWEAGSLELLRLKD 253
Cdd:PRK03918   293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklkelekrleelEERHELYEEAKAKKE 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  254 ENYMIAMRLAQLSEEKNSAVL-----RSRDLQLAVDQLKLKVSRLEEECALLR---------RGRGPPPGAE--EKEKEp 317
Cdd:PRK03918   373 ELERLKKRLTGLTPEKLEKELeelekAKEEIEEEISKITARIGELKKEIKELKkaieelkkaKGKCPVCGREltEEHRK- 451
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  318 dgvDLLSELRAENQRLTASLQELQEGLQQ----------EMSRPGAAGSERILLDI---------------LEHDWREAq 372
Cdd:PRK03918   452 ---ELLEEYTAELKRIEKELKEIEEKERKlrkelrelekVLKKESELIKLKELAEQlkeleeklkkynleeLEKKAEEY- 527
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  373 dsrQELCQKLHAVQGELQWAEelrdKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEI----EKERDQAIQSRDRI 448
Cdd:PRK03918   528 ---EKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPF 600
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1958789716  449 QLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLE 491
Cdd:PRK03918   601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
185-505 1.84e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  185 LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrLAQ 264
Cdd:COG4372     33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------LES 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  265 LSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaEEKEKEpdgvdlLSELRAENQRLTASLQELQEGL 344
Cdd:COG4372    106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------AEREEE------LKELEEQLESLQEELAALEQEL 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  345 QQEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDcdlykhrM 424
Cdd:COG4372    174 QALSEAEAEQALDELL--------KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA-------L 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  425 ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQGGSSLK 504
Cdd:COG4372    239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318

                   .
gi 1958789716  505 A 505
Cdd:COG4372    319 A 319
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-437 2.76e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  188 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIamrLAQLSE 267
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE---RASLEE 887
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  268 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLqqe 347
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELR-------------------EKLAQLELRLEGLEVRIDNLQERL--- 945
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  348 msrpgaAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLK-DCDLYKHRmAT 426
Cdd:TIGR02168  946 ------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAqKEDLTEAK-ET 1018
                          250
                   ....*....|.
gi 1958789716  427 VLAQLEEIEKE 437
Cdd:TIGR02168 1019 LEEAIEEIDRE 1029
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
198-498 3.70e-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: 41.31  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  198 SQLHREQQL-----------QARGRALEEERAGLEQRLREQQAAQERCQRL-------------REDWEAGSLELL---- 249
Cdd:pfam01576  468 SQLQDTQELlqeetrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlqaqlsdmkkKLEEDAGTLEALeegk 547
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  250 -RLKDEnymiAMRLAQLSEEKNSAV-----LRSR------DLQLAVDQLKLKVSRLE-----------EECALL-----R 301
Cdd:pfam01576  548 kRLQRE----LEALTQQLEEKAAAYdklekTKNRlqqeldDLLVDLDHQRQLVSNLEkkqkkfdqmlaEEKAISaryaeE 623
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  302 RGRGPppgAEEKEKEPDGVDLLSELRaENQRLTASLQELQEGLQQEM----SRPGAAGSErilLDILEHDWREAQDSRQE 377
Cdd:pfam01576  624 RDRAE---AEAREKETRALSLARALE-EALEAKEELERTNKQLRAEMedlvSSKDDVGKN---VHELERSKRALEQQVEE 696
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  378 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH-RTLLKDCDLYKHRMATVLAQLEEIE-------KERDQAIQSRDRIQ 449
Cdd:pfam01576  697 MKTQLEELEDELQATEDAKLRLEVNMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEaelederKQRAQAVAAKKKLE 776
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  450 LQYS--QSLIE-----KDQYRKQVRGLEAE--------------RDELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:pfam01576  777 LDLKelEAQIDaankgREEAVKQLKKLQAQmkdlqreleearasRDEILAQSKESEKKLKNLEAELLQLQ 846
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
321-498 4.79e-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: 40.52  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  321 DLLSELRAENQRLTASLQELQEgLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELqwAEELRDKYL 400
Cdd:COG4942     52 ALLKQLAALERRIAALARRIRA-LEQE-------------LAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYR 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  401 QEMEDlRLKH-------RTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 473
Cdd:COG4942    116 LGRQP-PLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
                          170       180
                   ....*....|....*....|....*
gi 1958789716  474 DELLTTVTSLEGTKAMLEAQLQRTQ 498
Cdd:COG4942    195 AERQKLLARLEKELAELAAELAELQ 219
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
157-476 5.13e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  157 FTLLTGQEPAQRCSMildeEGPEGLTQFLMTEVRRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQErcQR 236
Cdd:TIGR00618  572 FSILTQCDNRSKEDI----PNLQNITVRLQDLTEKLSEAEDMLA---CEQHALLRKLQPEQDLQDVRLHLQQCSQE--LA 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  237 LREDWEAGSLELLrLKDENYMIAMRLAQLSEEKNSAVLR------SRDLQLAVDQLKLKVSRLEEECALLRRGRGPPpga 310
Cdd:TIGR00618  643 LKLTALHALQLTL-TQERVREHALSIRVLPKELLASRQLalqkmqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR--- 718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  311 EEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQ---QEMSRPGAAGSERILLDIlehdwreaqdsrqELCQKLHAVQG 387
Cdd:TIGR00618  719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlKARTEAHFNNNEEVTAAL-------------QTGAELSHLAA 785
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  388 ELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYK----HRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYR 463
Cdd:TIGR00618  786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
                          330
                   ....*....|...
gi 1958789716  464 KQVRGLEAERDEL 476
Cdd:TIGR00618  866 QEQAKIIQLSDKL 878
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
73-150 5.39e-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: 37.19  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716   73 EDALWER-IEGVRHRLTRALNPAKLTPYLRQCrvLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRG-FEAFLEALE 150
Cdd:pfam16739    1 EDDEYRRlLRLFRPRLKDTIKPTEILPHLPEC--LTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGwFRAFLDALR 78
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
261-496 5.60e-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: 40.52  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  261 RLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgaeekekepdgvdlLSELRAENQRLTASLQEL 340
Cdd:COG4942     42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-------------------LAELEKEIAELRAELEAQ 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  341 QEGLQQ---EMSRPGAAGSERILLdilehdwreAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLkdc 417
Cdd:COG4942    103 KEELAEllrALYRLGRQPPLALLL---------SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789716  418 dlykhrmatvlAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 496
Cdd:COG4942    171 -----------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
202-442 7.36e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  202 REQQLQARGRALEEERAGLEQRLREqqaAQERCQRLREDweagsLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQL 281
Cdd:COG3206    169 RREEARKALEFLEEQLPELRKELEE---AEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  282 AVDQLKlkvSRLEEECALLRRGRGPPPGAEEKEKEpdgVDLLSELRAENQRLT----------ASLQELQEGLQQEMSRp 351
Cdd:COG3206    241 RLAALR---AQLGSGPDALPELLQSPVIQQLRAQL---AELEAELAELSARYTpnhpdvialrAQIAALRAQLQQEAQR- 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  352 gaagseriLLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLlkdcdlykhrmATVLAQL 431
Cdd:COG3206    314 --------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-----------ESLLQRL 374
                          250
                   ....*....|.
gi 1958789716  432 EEIEKERDQAI 442
Cdd:COG3206    375 EEARLAEALTV 385
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
176-268 7.48e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789716  176 EGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLRE----QQAAQERCQRLREDWEAGSLE-LLR 250
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEleekQQELEAQLEQLQEKAAETSQErKQK 217
                           90
                   ....*....|....*...
gi 1958789716  251 LKDENYMIAMRLaQLSEE 268
Cdd:PRK11448   218 RKEITDQAAKRL-ELSEE 234
 
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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