|
Name |
Accession |
Description |
Interval |
E-value |
| CARD_CARD10_CARMA3 |
cd08807 |
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ... |
27-112 |
1.38e-53 |
|
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260069 Cd Length: 86 Bit Score: 181.26 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08807 1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80
|
....*.
gi 1958789720 107 HFTLLT 112
Cdd:cd08807 81 HFTLLT 86
|
|
| CARD_CARD9-like |
cd08785 |
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ... |
27-112 |
5.97e-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: 142.13 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPcrANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08785 1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78
|
....*.
gi 1958789720 107 HFTLLT 112
Cdd:cd08785 79 LFTKVT 84
|
|
| CARD_CARD11_CARMA1 |
cd08808 |
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ... |
27-112 |
8.57e-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: 130.51 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08808 1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80
|
....*.
gi 1958789720 107 HFTLLT 112
Cdd:cd08808 81 LYKLVT 86
|
|
| CARD_CARD14_CARMA2 |
cd08806 |
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ... |
27-112 |
3.40e-24 |
|
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260068 Cd Length: 86 Bit Score: 97.25 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 27 LWERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:cd08806 1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80
|
....*.
gi 1958789720 107 HFTLLT 112
Cdd:cd08806 81 LYTQVT 86
|
|
| CARD_CARD9 |
cd08809 |
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ... |
28-112 |
5.37e-24 |
|
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260071 Cd Length: 86 Bit Score: 96.91 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 28 WERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 107
Cdd:cd08809 2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81
|
....*
gi 1958789720 108 FTLLT 112
Cdd:cd08809 82 YKKIT 86
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
28-114 |
6.19e-16 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.
Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 73.75 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 28 WERIEGVRHRLTRAL-NPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPE 106
Cdd:pfam00619 1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKAN---PTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77
|
....*...
gi 1958789720 107 HFTLLTGQ 114
Cdd:pfam00619 78 LASDLEGL 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-450 |
1.37e-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: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgAEEKEKEPDGVDLLSELRAENQRLTASLQELQEglqqe 298
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLE----- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 299 msrpgaagSERILLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKdcdlykhRMATV 378
Cdd:COG1196 370 --------AEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-------ALAEL 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789720 379 LAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| CARD |
cd01671 |
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
35-107 |
6.33e-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: 62.15 E-value: 6.33e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789720 35 RHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALEFYYPEH 107
Cdd:cd01671 5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSE---KTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPH 74
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-450 |
1.94e-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: 68.54 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 144 REARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQercQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSA 223
Cdd:TIGR02168 666 AKTNSSILERRREI----EELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 224 VLRSRDLQLAVDQLKLKVSRLEEECALLrrgrgpppgAEEKEKEPDgvdLLSELRAENQRLTASLQELQEGLQQEMSRPG 303
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEEL---------EERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 304 AAGSERILLDILEHDWREAqdsRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDlykhrmaTVLAQLE 383
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-------ELESELE 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789720 384 EIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-449 |
4.26e-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: 67.40 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 114 QEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQrlrEQQAAQERCQRLREDWE 193
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ---EEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 194 AGSLELLRLKDENYMIAMRLAQLSEEKNsavlrsrdlqlavdQLKLKVSRLEEEcallrrgrgpppgaEEKEKEPDGVDL 273
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLH--------------KLEEALNDLEAR--------------LSHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 274 LSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE 353
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 354 MEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLttvtS 433
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL----S 952
|
330
....*....|....*.
gi 1958789720 434 LEGTKAMLEAQLQRTQ 449
Cdd:TIGR02169 953 LEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-435 |
1.56e-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: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 141 RRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 220
Cdd:COG1196 262 LAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaeekekepdgVDLLSELRAENQRLTASLQELQEGLQQEMS 300
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---------------AEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 301 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 380
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958789720 381 QLEEiEKERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDELLTTVTSLE 435
Cdd:COG1196 485 ELAE-AAARLLLLLEAEADYEGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYE 537
|
|
| CARD_BCL10 |
cd08810 |
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ... |
29-101 |
1.66e-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: 55.43 E-value: 1.66e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789720 29 ERIEGVRHRLTRALNPAKLTPYLRQCRVLDEQDEEEVLSTyrfPCRANRTGRLIDILRCRGKRGFEAFLEALE 101
Cdd:cd08810 3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR---TTRKKRVDKLLDILAREGPDGLDALIESIR 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-449 |
2.62e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 173 QRLREQQAAQERCQRLREDWEAGSLELLRLKDENymIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallr 252
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLE----- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 253 rgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWRE----AQDSRQE 328
Cdd:COG1196 276 --------LEELELE------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 329 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLI 408
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958789720 409 EKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-437 |
1.49e-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: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 124 LDEEGPEGLTQF--LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRL-----------REQQAAQERCQRLRE 190
Cdd:TIGR02168 717 LRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeeelaeaeAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 191 DWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGppPGAEEKEKEPDG 270
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--ELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 271 VDLLSELRAENQRLTASLQELQEGLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDkY 350
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEE-------------LRELESKRSELRRELEELREKLAQLELRLEGLEVRID-N 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 351 LQEMedLRLKHRTLLKDcdlykhrmatVLAQLEEIEKERDQAIQSRDRIQLQYSQ-------SLIEKDQYRKQVRGLEAE 423
Cdd:TIGR02168 941 LQER--LSEEYSLTLEE----------AEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
|
330
....*....|....
gi 1958789720 424 RDELLTTVTSLEGT 437
Cdd:TIGR02168 1009 KEDLTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-450 |
2.00e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 142 RLREARKsQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELL-----RLKDENYMIAMRLAQL 216
Cdd:TIGR02168 173 RRKETER-KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 217 SEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 296
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEE-------------IEELQKE------LYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 297 QeMSRPGAAGSERIL-----LDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLY 371
Cdd:TIGR02168 313 N-LERQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789720 372 KHRMATVLAQLEEIEKERDQAIQSRDRiqLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
140-405 |
2.55e-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: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 140 VRRLREARK----SQLH------REQQLQARGRALEEERAGLEQRLREQQAAQERCQRL------------RED-WEAGS 196
Cdd:COG3096 419 VQALEKARAlcglPDLTpenaedYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQaWQTAR 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 197 lELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKlkvsrleeecALLRRGRGPPPGAEEKEkepdgvDLLSE 276
Cdd:COG3096 499 -ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----------EFCQRIGQQLDAAEELE------ELLAE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 277 LRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQklhavqgelQWAEELRDkyLQEMED 356
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE---------QSGEALAD--SQEVTA 630
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958789720 357 LrlkhrtllkdcdlykhrMATVLAQLEEIEKERDQAIQSRDRIQLQYSQ 405
Cdd:COG3096 631 A-----------------MQQLLEREREATVERDELAARKQALESQIER 662
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-427 |
2.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 138 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEA-----------GSLELLRLKDEN 206
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalllaglrglaGAVAVLIGVEAA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 207 YMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLK-LKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAENQRLT 285
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 286 ASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQD-----------SRQELCQKLHAVQGELQWAEELRDKYLQEM 354
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggSRRELLAALLEAEAELEELAERLAEEELEL 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 355 EDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEK-----------DQYRKQVRGLEAE 423
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELERLERE 775
|
....
gi 1958789720 424 RDEL 427
Cdd:COG1196 776 IEAL 779
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
162-435 |
3.80e-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: 51.11 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 162 RALEEERAGLEQRLrEQQAAQERCQRLREDWEAGSLELLR--------LKDENymIAMRLAQLSEEKNSAvlrsRDLQLA 233
Cdd:COG3096 839 AALRQRRSELEREL-AQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADET--LADRLEELREELDAA----QEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 234 VDQLKLKVSRLEEECALLRRgrgpPPGAEEkekepdgvdllsELRAENQRLTASLQELQEG---LQQEMSR--------- 301
Cdd:COG3096 912 IQQHGKALAQLEPLVAVLQS----DPEQFE------------QLQADYLQAKEQQRRLKQQifaLSEVVQRrphfsyeda 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 302 PGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELqwaeelrDKYLQEMEDLRLKHRTllkdcdlyKHRMATVLAQ 381
Cdd:COG3096 976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLASLKSSRDA--------KQQTLQELEQ 1040
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 382 -LEEIEKERD-----QAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 435
Cdd:COG3096 1041 eLEELGVQADaeaeeRARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-447 |
4.48e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 162 RALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDenymiamRLAQLSEEKNSAvLRSRDLQLAVDQLKLKV 241
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRREREKA-ERYQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 242 SRLEEEcallrrgrgpppgAEEKEKEpdgvdllsELRAENQRLTASLQELQEGLQQEMSRPGAAgsERILLDILEHDWRE 321
Cdd:TIGR02169 228 LLKEKE-------------ALERQKE--------AIERQLASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 322 AQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQ---AIQSRD- 397
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKe 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 398 -----RIQLQ-----YSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 447
Cdd:TIGR02169 365 eledlRAELEevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-301 |
4.67e-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: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 141 RRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQERCQRLRE------DWEAGSLELLRLKDE-------NY 207
Cdd:COG4913 609 RAKLAALEAEL---AELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAElerldasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 208 MIA---MRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDLLSELRAEN--Q 282
Cdd:COG4913 686 DLAaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAveR 765
|
170
....*....|....*....
gi 1958789720 283 RLTASLQELQEGLQQEMSR 301
Cdd:COG4913 766 ELRENLEERIDALRARLNR 784
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
155-435 |
6.25e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 155 QQLQARGRALEEERAGlEQRLREQ-QAAQERCQRLREdwEAGSLELLrlkDENYMIAmRLAQLSEEKNSAVLRSRDLQL- 232
Cdd:PRK04863 844 RRRVELERALADHESQ-EQQQRSQlEQAKEGLSALNR--LLPRLNLL---ADETLAD-RVEEIREQLDEAEEAKRFVQQh 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 233 --AVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPD-GVDLLSELRA--------ENQRLTASLQELQEGLQQEMSR 301
Cdd:PRK04863 917 gnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqQAFALTEVVQrrahfsyeDAAEMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 302 pgaAGSERillDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLkhrtllkdcdlykhrmaTVLAQ 381
Cdd:PRK04863 997 ---AEQER---TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGV-----------------PADSG 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958789720 382 LEEiekerdQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLE 435
Cdd:PRK04863 1054 AEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-450 |
7.79e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 145 EARKSQLHRE-QQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrlaqlseeknsa 223
Cdd:TIGR02168 273 RLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE------------------ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 224 vlrsrdLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLQQEMSRpg 303
Cdd:TIGR02168 335 ------LAEELAELEEKLEELKEELESLE-------------------AELEELEAELEELESRLEELEEQLETLRSK-- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 304 aagserilLDILEHDWREAQDSRQELCQKLHAVQGElqwaeelRDKYLQEMEDLRLKhrtllkdcdLYKHRMATVLAQLE 383
Cdd:TIGR02168 388 --------VAQLELQIASLNNEIERLEARLERLEDR-------RERLQQEIEELLKK---------LEEAELKELQAELE 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789720 384 EIEKERDQAIQSRDRIQLQYSQSliekdqyRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQG 450
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEEL-------REELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-453 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 141 RRLREARKSQLHREQQlqargrALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymIAMRLAQLSEEk 220
Cdd:TIGR02169 218 KEKREYEGYELLKEKE------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE---LNKKIKDLGEE- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 221 nsavlRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQQEms 300
Cdd:TIGR02169 288 -----EQLRVKEKIGELEAEIASLERSIAEKERE------LEDAEER------LAKLEAEIDKLLAEIEELEREIEEE-- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 301 rpgaagseRILLDILEHDWREAQDSRQELCQKLHAVQGELQ-WAEELR------DKYLQEMEDL-----RLKHRTLLKDC 368
Cdd:TIGR02169 349 --------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKdyreklEKLKREINELkreldRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 369 DLYKHRM--ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQ 446
Cdd:TIGR02169 421 ELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
330
....*....|
gi 1958789720 447 ---RTQGGSS 453
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 ... |
153-453 |
2.16e-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: 48.63 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 153 REQQLQARGRALEEERAGLEQRLREQQAAQERCQ--RLREDWEAGSLE--LLRLKDENY-------MIAMRLAQLS---- 217
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQleKVTTEAKIKKLEedILLLEDQNSklskerkLLEERISEFTsnla 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 218 --EEKNSAVLRSRDLQLAV-----DQLKlKVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSELRAENQRLTASLQE 290
Cdd:pfam01576 170 eeEEKAKSLSKLKNKHEAMisdleERLK-KEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 291 LQEGLQQEMSRPGAAGS-----ERILLDILEHDWRE------AQDSRQELCQKLHAVQGELQ-------WAEELRDKYLQ 352
Cdd:pfam01576 248 ALARLEEETAQKNNALKkirelEAQISELQEDLESEraarnkAEKQRRDLGEELEALKTELEdtldttaAQQELRSKREQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 353 EMEDLRlkhRTLLKDCDLYKhrmatvlAQLEEIEKERDQAIqsrDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVT 432
Cdd:pfam01576 328 EVTELK---KALEEETRSHE-------AQLQEMRQKHTQAL---EELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
330 340
....*....|....*....|....*...
gi 1958789720 433 SLEGTKA-------MLEAQLQRTQGGSS 453
Cdd:pfam01576 395 TLQQAKQdsehkrkKLEGQLQELQARLS 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
138-358 |
2.17e-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: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 138 TEVRRLREARKSQLHRE--QQLQARGRALEEERAGLEQRLREQQA----AQERCQRLREDWEAGSLEllrlkdenymiam 211
Cdd:COG4913 272 AELEYLRAALRLWFAQRrlELLEAELEELRAELARLEAELERLEArldaLREELDELEAQIRGNGGD------------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 212 RLAQLSEEKnsavlrsRDLQLAVDQLKLKVSRLEEECALLrrGRGPPPGAEEkekepdgvdlLSELRAENQRLTASLQEL 291
Cdd:COG4913 339 RLEQLEREI-------ERLERELEERERRRARLEALLAAL--GLPLPASAEE----------FAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789720 292 QEGLQQEMsrpgaagserilldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 358
Cdd:COG4913 400 LEALEEAL--------------------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
143-245 |
2.22e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 143 LREARkSQLHREQQLQARGRALEEeragLEQRLREQQAAQER----CQRLREDWEAGS-LELLRLKDEnymiaMRLAQLS 217
Cdd:PRK04863 502 LRRLR-EQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLlaefCKRLGKNLDDEDeLEQLQEELE-----ARLESLS 571
|
90 100
....*....|....*....|....*...
gi 1958789720 218 EEKNSAVLRSRDLQLAVDQLKLKVSRLE 245
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLA 599
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-362 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 137 MTEVRRLREARKSQLHREQQLqargRALEEERAGLEQRLREQQAAQERCQRlredweagSLELLRLKDENYMIAMRLAQL 216
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE--------ELEKLEKLLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 217 SEEknsavlrsrdlqlavdqLKLKVSRLEEecallrrgrgpppgAEEKEKEpdgvdlLSELRAENQRLTASLQELQEGLQ 296
Cdd:COG4717 138 EAE-----------------LAELPERLEE--------------LEERLEE------LRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958789720 297 QEMSRPGAAGSERiLLDILEhDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHR 362
Cdd:COG4717 181 ELLEQLSLATEEE-LQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-298 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 130 EGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMI 209
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 210 AMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRgrgpppgAEEKEKEpdgvdLLSELRAENQRLTASLQ 289
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAE-----EEAELEEEEEALLELLA 466
|
....*....
gi 1958789720 290 ELQEGLQQE 298
Cdd:COG1196 467 ELLEEAALL 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-449 |
3.11e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRR-----------------------------------GRGPPPGAEE 263
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaarllllleaeadyegflegvkaalllaglRGLAGAVAVL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 264 --KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQ 341
Cdd:COG1196 530 igVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 342 WAEELRDKYLQEMEDLRLKHRTLlkdcDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLE 421
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
330 340
....*....|....*....|....*...
gi 1958789720 422 AERDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAE 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-442 |
3.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSL-ELLRLKDENYMIAMRLAQLS 217
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 218 EEKNSAVLRSRDLQLAVDQLKLKVSRLEEE----------------CALLRRGRGPPPGAEE------------------ 263
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalLALLGLGGSLLSLILTiagvlflvlgllallfll 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 264 -KEKEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQW 342
Cdd:COG4717 293 lAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 343 AEELRDKYLQEMEDLRLKHRTLLKDCDLyKHRMATVLAQLEEIEKERDQAIQSRDRIQLQysqslIEKDQYRKQVRGLEA 422
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEE 446
|
330 340
....*....|....*....|
gi 1958789720 423 ERDELLTTVTSLEGTKAMLE 442
Cdd:COG4717 447 ELEELREELAELEAELEQLE 466
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
115-442 |
4.30e-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: 47.66 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 115 EPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEEraglEQRLREQQAAQERC-QRLREDWE 193
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCdNRSKEDIP 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 194 AGSLELLRLKDENYMIAMRLAQLSEEkNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVDL 273
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 274 LSELRAEN-QRLTASLQELQEGLQQEMS-RPGAAGSERILLDILEH---DWREaqdsRQELCQKLHAVQGELQWAEELRD 348
Cdd:TIGR00618 667 IRVLPKELlASRQLALQKMQSEKEQLTYwKEMLAQCQTLLRELETHieeYDRE----FNEIENASSSLGSDLAAREDALN 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 349 KYLQEMEDLR---LKHRTLLKDCDLYKHRMA-TVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:TIGR00618 743 QSLKELMHQArtvLKARTEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
330
....*....|....*...
gi 1958789720 425 DELLttVTSLEGTKAMLE 442
Cdd:TIGR00618 823 CETL--VQEEEQFLSRLE 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-427 |
5.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 120 CSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGlEQRLREQQAAQERCQRLREDWEAGSLEL 199
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 200 LRLKDENYmiamrlaqlseEKnsavLRSRDLQLAVDQLKLKvSRLEEECALLRRGRGPPPGAEEKEKEPDgvDLLSELRA 279
Cdd:PRK03918 520 LEKKAEEY-----------EK----LKEKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELA--ELLKELEE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 280 EN----QRLTASLQELQEGLQQEMSRPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQE-M 354
Cdd:PRK03918 582 LGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeY 661
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789720 355 EDLRLKHRTLLKdcdlykhRMATVLAQLEEIEKERDQAIQSRDRIQLQysqsLIEKDQYRKQVRGLEAERDEL 427
Cdd:PRK03918 662 EELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERV 723
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-317 |
5.19e-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: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENymiamRLAQLSE 218
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-----RFAAALG 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 219 EKNSAVLRsRDLQLAVDQLKLKVSRLEEECALLRRG---RGPPPGAE---EKEKEPDGVDLLSELRAEN---------QR 283
Cdd:COG4913 761 DAVERELR-ENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADldaDLESLPEYLALLDRLEEDGlpeyeerfkEL 839
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958789720 284 LTASLQELQEGLQQEMSRPGAAGSERI--LLDILEH 317
Cdd:COG4913 840 LNENSIEFVADLLSKLRRAIREIKERIdpLNDSLKR 875
|
|
| SH3_ZO-1 |
cd12026 |
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ... |
735-800 |
6.17e-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: 6.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789720 735 EPFYIRANFSLpERADPHALCVKAQEILRLVDPAYK-RRQEWFCTRVDTlTLRDLDRGTVPNYQRAQ 800
Cdd:cd12026 1 DSFYIRTHFEY-EKESPYGLSFNKGEVFRVVDTLYNgKLGSWLAIRIGK-NHKEVERGIIPNKNRAE 65
|
|
| SH3_ZO |
cd11859 |
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ... |
738-800 |
8.22e-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: 8.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789720 738 YIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 800
Cdd:cd11859 1 YIRTHFDY-EKPAKGELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-374 |
1.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 121 SMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLqargRALEEERAGLE--QRLREQQAAQERCQRLREDWEAgSLE 198
Cdd:COG4913 215 EYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAEryAAARERLAELEYLRAALRLWFA-QRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 199 LLRLKDEnymiamrLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEEcallRRGrgpppgaeekekepDGVDLLSELR 278
Cdd:COG4913 290 LELLEAE-------LEELRAELARLEAELERLEARLDALREELDELEAQ----IRG--------------NGGDRLEQLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 279 AENQRLTASLQELQEGLQQEMSRPGAAGSErilldiLEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR 358
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLP------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
250
....*....|....*.
gi 1958789720 359 LKHRTLLKDCDLYKHR 374
Cdd:COG4913 419 RELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-427 |
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: 46.26 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 137 MTEVRRLREARKSQLhrEQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRlaql 216
Cdd:pfam15921 333 LREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 217 sEEKNSAVLRSrdLQLAVDQLKLKVSRLEeecALLRRGRGPPPGAEEKEkepdgvdlLSELRAENQ------RLTASLQE 290
Cdd:pfam15921 407 -DTGNSITIDH--LRRELDDRNMEVQRLE---ALLKAMKSECQGQMERQ--------MAAIQGKNEslekvsSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 291 LQEGLQQEMSRPGAagsERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH---RTLLKD 367
Cdd:pfam15921 473 TKEMLRKVVEELTA---KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTE 549
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789720 368 CDLYKHRMAtvlAQLEEIEKERDQaIQSRDRIQLQYSQS----LIEKDQYRKQVRGLEAERDEL 427
Cdd:pfam15921 550 CEALKLQMA---EKDKVIEILRQQ-IENMTQLVGQHGRTagamQVEKAQLEKEINDRRLELQEF 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-449 |
1.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAgSLELLRLKDENYMIAMRLAQLSE 218
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 219 EknsaVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgppPGAEEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQQ- 297
Cdd:COG4717 154 R----LEELRELEEELEELEAELAELQEELEELLEQ----LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEl 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 298 -------EMSRPGAAGSERI-----------LLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRL 359
Cdd:COG4717 226 eeeleqlENELEAAALEERLkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 360 KHRTLLKDCDLYKHRMATVLAQLE-EIEKERDQAIQSRDRI-QLQYSQSLIEKDQYRKQVRGLEAERDELLTT--VTSLE 435
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIeELQELLREAEELEEELQLEELEQEIAALLAEagVEDEE 385
|
330
....*....|....
gi 1958789720 436 GTKAMLEAQLQRTQ 449
Cdd:COG4717 386 ELRAALEQAEEYQE 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-427 |
1.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 271 VDLLSELRAENQRLTASLQELQEgLQQEMSRPGAAGSERIL------LDILEHDWREAQDSRQELCQKLHAVQGELqwaE 344
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQRRLelleaeLEELRAELARLEAELERLEARLDALREEL---D 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 345 ELRDKYLQ-----------EMEDLRLKHRTLLKDCDLYKHRMATV-----------LAQLEEIEKERDQAIQSRDRIQLQ 402
Cdd:COG4913 327 ELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*
gi 1958789720 403 YSQSLIEKDQYRKQVRGLEAERDEL 427
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASL 431
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-475 |
1.85e-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: 45.73 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 141 RRLREARKSQLHREQQLQARGRALEEERAgLEQRLREQQAAQERcqrlREDWEAGSLELLRLKDENYMIAMRLAQLSEEK 220
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRA-QEAVLEETQERINR----ARKAAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 221 NS-AVLRSRDLQLAVDQLKLKVSR-----LEEECALLRRGRGPPPG-AEEKEKEpdgVDLLSELRAENQRLTASLQELQe 293
Cdd:TIGR00618 321 RSrAKLLMKRAAHVKQQSSIEEQRrllqtLHSQEIHIRDAHEVATSiREISCQQ---HTLTQHIHTLQQQKTTLTQKLQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 294 glqqemsrpgAAGSERILLDILEHDwREAQDSRQE-LCQKLHAVQGElqwaEELRDKYLQEMEDLRLKHRTLLKDCDLYK 372
Cdd:TIGR00618 397 ----------SLCKELDILQREQAT-IDTRTSAFRdLQGQLAHAKKQ----QELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 373 HRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR-TQGG 451
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLE 541
|
330 340
....*....|....*....|....
gi 1958789720 452 SSLKacASSHSLCSNLSSTWSLSE 475
Cdd:TIGR00618 542 TSEE--DVYHQLTSERKQRASLKE 563
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-449 |
2.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 142 RLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEK- 220
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEl 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKEPDGVD-LLSELRAENQRLTASLQELQEGLQQEM 299
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKeARLLLLIAAALLALLGLGGSLLSLILT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 300 SRPGAAGSERILLDILEHDWREAQDSRQELcQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVL 379
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEA-EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 380 AQLEEIEKERDQAIQSRDRIQL----------QYSQSLIEKDQY---RKQVRGLEAERDELLTTVTSL--EGTKAMLEAQ 444
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYqelKEELEELEEQLEELLGELEELleALDEEELEEE 433
|
....*
gi 1958789720 445 LQRTQ 449
Cdd:COG4717 434 LEELE 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
241-424 |
2.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 241 VSRLEEECALLRRGRGPPP-----GAEEKEKEpdgVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGSERILLDIL 315
Cdd:COG4717 48 LERLEKEADELFKPQGRKPelnlkELKELEEE---LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 316 E------HDWREAQDSRQELCQKLHAVQGELQWAEELRDKY---LQEMEDLRLKHRTLLKDCDLYKH-RMATVLAQLEEI 385
Cdd:COG4717 125 LqllplyQELEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEeELQDLAEELEEL 204
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958789720 386 EKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-445 |
3.43e-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: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 327 QELCQKLHAVQGELQWAEELRDKylQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQS 406
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958789720 407 -LIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQL 445
Cdd:COG4913 336 gGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
261-412 |
4.29e-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: 42.59 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 261 AEEKEKEPDGVDLLSELRAENQRLTASLQELQ---EGLQQEMsrpgaAGSER---IL------LDILEHDWREAQDSRQE 328
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQeevEELRKQL-----ENYEKdkqSLknlkarLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 329 LCQKLHAVQGELQwaeELRDKYLQEMEDLRLKhrTLLKDCdLYKHRMATVLAQLEEIEKERDQAIQS-------RDRIQL 401
Cdd:pfam13851 111 LEQRFEKVERERD---ELYDKFEAAIQDVQQK--TGLKNL-LLEKKLQALGETLEKKEAQLNEVLAAanldpdaLQAVTE 184
|
170
....*....|.
gi 1958789720 402 QYSQSLIEKDQ 412
Cdd:pfam13851 185 KLEDVLESKNQ 195
|
|
| SH3_ZO-3 |
cd12028 |
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ... |
737-800 |
4.44e-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: 4.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958789720 737 FYIRANFSLpERADPHALCVKAQEILRLVDPAYKRR-QEWFCTRVDTlTLRDLDRGTVPNYQRAQ 800
Cdd:cd12028 3 FYIRTHFDY-EPDPPSGLSFTRGEVFHVLDTMHRGKlGSWLAVRMGR-DLREMEKGIIPNQSRAE 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-393 |
5.20e-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: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAA----QERCQRLREDWEAGSLELLRLKDENYMIAMRLA 214
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 215 QLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALL--RRGRgpppgaEEKEKEPDGVDLLSELRAENQRLTASLQELQ 292
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedRRER------LQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 293 EGLQQEMSRPGAAgserilLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLR--LKHRTLLKDcdl 370
Cdd:TIGR02168 450 EELQEELERLEEA------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSG--- 520
|
250 260
....*....|....*....|...
gi 1958789720 371 ykhrMATVLAQLEEIEKERDQAI 393
Cdd:TIGR02168 521 ----ILGVLSELISVDEGYEAAI 539
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-426 |
6.41e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERA-GLEQRLREQQAAQERCQRLREDWEAGslELLRLKDENYMIAMRLAQLS 217
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAeEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAA 1506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 218 EEKNSAvlrsRDLQLAVDQLKLKVSRLEEEcallRRGRGPPPGAEEKEKEpdgvdllSELR-AENQRLTASLQELQEGLQ 296
Cdd:PTZ00121 1507 EAKKKA----DEAKKAEEAKKADEAKKAEE----AKKADEAKKAEEKKKA-------DELKkAEELKKAEEKKKAEEAKK 1571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 297 QEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQwAEELRDKylqemEDLRLKHRTLLKDCDLYKHRMA 376
Cdd:PTZ00121 1572 AEEDKNMALRKAEEA--------KKAEEARIEEVMKLYEEEKKMK-AEEAKKA-----EEAKIKAEELKKAEEEKKKVEQ 1637
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958789720 377 TVLAQLEEIEK-ERDQAIQSRDRIQLQYSQSLIEKDQyRKQVRGLEAERDE 426
Cdd:PTZ00121 1638 LKKKEAEEKKKaEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDE 1687
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-428 |
8.22e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 141 RRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREdweagslELLRLKDENYMIAMRLAQLSEEK 220
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 221 NSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRGPPPGAEEKEKepdgvdlLSELRAENQRLTASLQELQEGLQQEMS 300
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-------LDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 301 RPGAAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLA 380
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958789720 381 QLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELL 428
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-446 |
1.18e-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: 43.03 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 107 HFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLHREQQLQ-----------------ARGRALEEERA 169
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqihlqetrkkavvlARLLELQEEPC 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 170 GLEQRLREQQAA----------QERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKL 239
Cdd:TIGR00618 505 PLCGSCIHPNPArqdidnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 240 KVSRLEEECALLRRgRGPPPGAEEKEKEPDGVDLLSEL--RAENQRLTASLQELQEGLQQEMsrpgaAGSERILLDILEH 317
Cdd:TIGR00618 585 DIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKLqpEQDLQDVRLHLQQCSQELALKL-----TALHALQLTLTQE 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 318 DWREA-QDSRQELCQKLHAVQGELQ-----------WAEEL--RDKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQ-- 381
Cdd:TIGR00618 659 RVREHaLSIRVLPKELLASRQLALQkmqsekeqltyWKEMLaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAre 738
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958789720 382 ------LEEIEKERDQAIQSRDRIQLQYSQSLI----EKDQYRKQVRGLEAERDELLTTVTSLegtkAMLEAQLQ 446
Cdd:TIGR00618 739 dalnqsLKELMHQARTVLKARTEAHFNNNEEVTaalqTGAELSHLAAEIQFFNRLREEDTHLL----KTLEAEIG 809
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-442 |
1.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 138 TEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLR-------------EDWEAGSLELLRLKD 204
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklkelekrleelEERHELYEEAKAKKE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 205 ENYMIAMRLAQLSEEKNSAVL-----RSRDLQLAVDQLKLKVSRLEEECALLR---------RGRGPPPGAE--EKEKEp 268
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELeelekAKEEIEEEISKITARIGELKKEIKELKkaieelkkaKGKCPVCGREltEEHRK- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 269 dgvDLLSELRAENQRLTASLQELQEGLQQ----------EMSRPGAAGSERILLDI---------------LEHDWREAq 323
Cdd:PRK03918 452 ---ELLEEYTAELKRIEKELKEIEEKERKlrkelrelekVLKKESELIKLKELAEQlkeleeklkkynleeLEKKAEEY- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 324 dsrQELCQKLHAVQGELQWAEelrdKYLQEMEDLRLKHRTLLKDCDLYKHRMATVLAQLEEI----EKERDQAIQSRDRI 399
Cdd:PRK03918 528 ---EKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPF 600
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958789720 400 QLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLE 442
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-456 |
2.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 136 LMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDEnymiamrLAQ 215
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------LES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 216 LSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGRgpppgaEEKEKEpdgvdlLSELRAENQRLTASLQELQEGL 295
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------AEREEE------LKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 296 QQEMSRPGAAGSERILldilehdwREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLKDcdlykhrM 375
Cdd:COG4372 174 QALSEAEAEQALDELL--------KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA-------L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 376 ATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQRTQGGSSLK 455
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
.
gi 1958789720 456 A 456
Cdd:COG4372 319 A 319
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-388 |
2.71e-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: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 139 EVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLREQQAAQERCQRLREDWEAGSLELLRLKDENYMIamrLAQLSE 218
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE---RASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 219 EKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRrgrgpppgaeekekepdgvDLLSELRAENQRLTASLQELQEGLqqe 298
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELR-------------------EKLAQLELRLEGLEVRIDNLQERL--- 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 299 msrpgaAGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLK-DCDLYKHRmAT 377
Cdd:TIGR02168 946 ------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAqKEDLTEAK-ET 1018
|
250
....*....|.
gi 1958789720 378 VLAQLEEIEKE 388
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 ... |
149-449 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 149 SQLHREQQL-----------QARGRALEEERAGLEQRLREQQAAQERCQRL-------------REDWEAGSLELL---- 200
Cdd:pfam01576 468 SQLQDTQELlqeetrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlqaqlsdmkkKLEEDAGTLEALeegk 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 201 -RLKDEnymiAMRLAQLSEEKNSAV-----LRSR------DLQLAVDQLKLKVSRLE-----------EECALL-----R 252
Cdd:pfam01576 548 kRLQRE----LEALTQQLEEKAAAYdklekTKNRlqqeldDLLVDLDHQRQLVSNLEkkqkkfdqmlaEEKAISaryaeE 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 253 RGRGPppgAEEKEKEPDGVDLLSELRaENQRLTASLQELQEGLQQEM----SRPGAAGSErilLDILEHDWREAQDSRQE 328
Cdd:pfam01576 624 RDRAE---AEAREKETRALSLARALE-EALEAKEELERTNKQLRAEMedlvSSKDDVGKN---VHELERSKRALEQQVEE 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 329 LCQKLHAVQGELQWAEELRDKYLQEMEDLRLKH-RTLLKDCDLYKHRMATVLAQLEEIE-------KERDQAIQSRDRIQ 400
Cdd:pfam01576 697 MKTQLEELEDELQATEDAKLRLEVNMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEaelederKQRAQAVAAKKKLE 776
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 401 LQYS--QSLIE-----KDQYRKQVRGLEAE--------------RDELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:pfam01576 777 LDLKelEAQIDaankgREEAVKQLKKLQAQmkdlqreleearasRDEILAQSKESEKKLKNLEAELLQLQ 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-449 |
5.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 272 DLLSELRAENQRLTASLQELQEgLQQEmsrpgaagserilLDILEHDWREAQDSRQELCQKLHAVQGELqwAEELRDKYL 351
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRA-LEQE-------------LAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 352 QEMEDlRLKH-------RTLLKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAER 424
Cdd:COG4942 116 LGRQP-PLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180
....*....|....*....|....*
gi 1958789720 425 DELLTTVTSLEGTKAMLEAQLQRTQ 449
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQ 219
|
|
| CARD_2 |
pfam16739 |
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ... |
29-101 |
5.96e-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: 5.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958789720 29 ERIEGVRHRLTRALNPAKLTPYLRQCrvLDEQDEEEVLSTYRFPCRANRTGRLIDILRCRGKRG-FEAFLEALE 101
Cdd:pfam16739 7 RLLRLFRPRLKDTIKPTEILPHLPEC--LTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGwFRAFLDALR 78
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
212-447 |
6.72e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 212 RLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRGrgpppgaeekekepdgvdlLSELRAENQRLTASLQEL 291
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-------------------LAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 292 QEGLQQ---EMSRPGAAGSERILLdilehdwreAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLLkdc 368
Cdd:COG4942 103 KEELAEllrALYRLGRQPPLALLL---------SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789720 369 dlykhrmatvlAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTVTSLEGTKAMLEAQLQR 447
Cdd:COG4942 171 -----------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-427 |
6.90e-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: 40.72 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 108 FTLLTGQEPAQRCSMildeEGPEGLTQFLMTEVRRLREARKSQLhreQQLQARGRALEEERAGLEQRLREQQAAQErcQR 187
Cdd:TIGR00618 572 FSILTQCDNRSKEDI----PNLQNITVRLQDLTEKLSEAEDMLA---CEQHALLRKLQPEQDLQDVRLHLQQCSQE--LA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 188 LREDWEAGSLELLrLKDENYMIAMRLAQLSEEKNSAVLR------SRDLQLAVDQLKLKVSRLEEECALLRRGRGPPpga 261
Cdd:TIGR00618 643 LKLTALHALQLTL-TQERVREHALSIRVLPKELLASRQLalqkmqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR--- 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 262 EEKEKEPDGVDLLSELRAENQRLTASLQELQEGLQ---QEMSRPGAAGSERILLDIlehdwreaqdsrqELCQKLHAVQG 338
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlKARTEAHFNNNEEVTAAL-------------QTGAELSHLAA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 339 ELQWAEELRDKYLQEMEDLRLKHRTLLKDCDLYK----HRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYR 414
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
330
....*....|...
gi 1958789720 415 KQVRGLEAERDEL 427
Cdd:TIGR00618 866 QEQAKIIQLSDKL 878
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
127-219 |
7.35e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 127 EGPEGLTQFLMTEVRRLREARKSQLHREQQLQARGRALEEERAGLEQRLRE----QQAAQERCQRLREDWEAGSLE-LLR 201
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEleekQQELEAQLEQLQEKAAETSQErKQK 217
|
90
....*....|....*...
gi 1958789720 202 LKDENYMIAMRLaQLSEE 219
Cdd:PRK11448 218 RKEITDQAAKRL-ELSEE 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
153-393 |
9.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 153 REQQLQARGRALEEERAGLEQRLREqqaAQERCQRLREDweagsLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQL 232
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEE---AEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 233 AVDQLKlkvSRLEEECALLRRGRGPPPGAEEKEKEpdgVDLLSELRAENQRLT----------ASLQELQEGLQQEMSRp 302
Cdd:COG3206 241 RLAALR---AQLGSGPDALPELLQSPVIQQLRAQL---AELEAELAELSARYTpnhpdvialrAQIAALRAQLQQEAQR- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 303 gaagseriLLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDKYLQEMEDLRLKHRTLlkdcdlykhrmATVLAQL 382
Cdd:COG3206 314 --------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-----------ESLLQRL 374
|
250
....*....|.
gi 1958789720 383 EEIEKERDQAI 393
Cdd:COG3206 375 EEARLAEALTV 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-435 |
9.77e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 262 EEKEkEPDGVDLLSELRAENQRLTASLQELQEGLQQEMSRPGAAGserillDILEhDWREAQDSRQELCQKLHAVQGELQ 341
Cdd:PRK02224 197 EEKE-EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD------EVLE-EHEERREELETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789720 342 WAEELRDKYLQEMEDLRLKHRTL-------LKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYR 414
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELeeerddlLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180
....*....|....*....|.
gi 1958789720 415 KQVRGLEAERDELLTTVTSLE 435
Cdd:PRK02224 349 EDADDLEERAEELREEAAELE 369
|
|
| |
