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Conserved domains on  [gi|15234086|ref|NP_192027|]
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XH/XS domain-containing protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 29-141 3.13e-49

XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins including gene X and SGS3. SGS3 is thought to be involved in post-transcriptional gene silencing (PTGS). This domain contains a conserved aspartate residue that may be functionally important. The XS domain has recently been predicted to possess an RRM-like RNA-binding domain by fold recognition.


:

Pssm-ID: 460933  Cd Length: 113  Bit Score: 165.81  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    29 QKRYVWPWVGLVANVPTEVEPSGRRVGKSGSTLRDEFtlKGFNPTRVKPIWNTKGHTGFALVEFAKDFKGFESAMQFEKS 108
Cdd:pfam03468   1 DELFVWPWMGIVVNIPTEQDEDGRWVGMSGEELKDKL--SRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKH 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15234086   109 FDLDRHGKRDW-KKGHRLRDDKLYGWLAREDDYN 141
Cdd:pfam03468  79 FEAQGHGKKDWgGKRNRGSGSKLYGWVARADDYN 112
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 410-550 1.14e-45

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


:

Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 156.98  E-value: 1.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   410 KIMGELNPAPFLPAVMNKH-------KAMMLCSVWAAEIGDVQWTPFRVDESDGTPKQklhisqhskcemqrVVDENDEK 482
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFsneeaevKAAELCSLWEEELKDPEWHPFKVVMVDGKHKE--------------VIDEDDEK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234086   483 LRMLKNQYGEEVYSEVVRAKLEMEEHNASGSYETEELWNYEENRKATIEEITDVMLKirsKLAAMKNK 550
Cdd:pfam03469  67 LKELKEEYGEEVYNAVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILK---QWKALKRK 131
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
178-403 1.01e-05

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  178 CQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEKNMQEfyqqvlggheksfaELEAKREKLDERARLIE 257
Cdd:COG5022  873 SAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE--------------NLEFKTELIARLKKLLN 938

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  258 QRAIKNEEEMEKTRLEREM-IQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQELELEIEKLKGTTNVM 336
Cdd:COG5022  939 NIDLEEGPSIEYVKLPELNkLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL 1018

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234086  337 KHMVGCDGDKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDA--RKEMIKVWKANEELMK 403
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALklRRENSLLDDKQLYQLE 1087
 
Name Accession Description Interval E-value
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 29-141 3.13e-49

XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins including gene X and SGS3. SGS3 is thought to be involved in post-transcriptional gene silencing (PTGS). This domain contains a conserved aspartate residue that may be functionally important. The XS domain has recently been predicted to possess an RRM-like RNA-binding domain by fold recognition.


Pssm-ID: 460933  Cd Length: 113  Bit Score: 165.81  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    29 QKRYVWPWVGLVANVPTEVEPSGRRVGKSGSTLRDEFtlKGFNPTRVKPIWNTKGHTGFALVEFAKDFKGFESAMQFEKS 108
Cdd:pfam03468   1 DELFVWPWMGIVVNIPTEQDEDGRWVGMSGEELKDKL--SRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKH 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15234086   109 FDLDRHGKRDW-KKGHRLRDDKLYGWLAREDDYN 141
Cdd:pfam03468  79 FEAQGHGKKDWgGKRNRGSGSKLYGWVARADDYN 112
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 32-140 4.09e-49

RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important.


Pssm-ID: 409710  Cd Length: 107  Bit Score: 165.22  E-value: 4.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  32 YVWPWVGLVANVPTEVEPSGRRVGKSGSTLRDEftLKGFNPTRVKPIWNTKGHTGFALVEFAKDFKGFESAMQFEKSFDL 111
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDNRKMEGGSNKELLER--LIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEV 78

                        90       100
                ....*....|....*....|....*....
gi 15234086 112 DRHGKRDWKKGHRLRDDKLYGWLAREDDY 140
Cdd:cd12266  79 DGHGKKDWRNKKGGRKSKLYGWLARADDY 107
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 410-550 1.14e-45

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 156.98  E-value: 1.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   410 KIMGELNPAPFLPAVMNKH-------KAMMLCSVWAAEIGDVQWTPFRVDESDGTPKQklhisqhskcemqrVVDENDEK 482
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFsneeaevKAAELCSLWEEELKDPEWHPFKVVMVDGKHKE--------------VIDEDDEK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234086   483 LRMLKNQYGEEVYSEVVRAKLEMEEHNASGSYETEELWNYEENRKATIEEITDVMLKirsKLAAMKNK 550
Cdd:pfam03469  67 LKELKEEYGEEVYNAVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILK---QWKALKRK 131
COG5022 COG5022
Myosin heavy chain [General function prediction only];
178-403 1.01e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  178 CQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEKNMQEfyqqvlggheksfaELEAKREKLDERARLIE 257
Cdd:COG5022  873 SAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE--------------NLEFKTELIARLKKLLN 938

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  258 QRAIKNEEEMEKTRLEREM-IQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQELELEIEKLKGTTNVM 336
Cdd:COG5022  939 NIDLEEGPSIEYVKLPELNkLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL 1018

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234086  337 KHMVGCDGDKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDA--RKEMIKVWKANEELMK 403
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALklRRENSLLDDKQLYQLE 1087
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-401 4.58e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    151 KKKRDLKSISQIVEEDQRKLYHLFENMCQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNsYQEEIQKMEKNMQEFyQQ 230
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-LKEELKALREALDEL-RA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    231 VLGGHEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIM 310
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    311 ----EMEAKLNETQELELEIEKLKGTTNVMKHMVGcdgdkDIVEKIAKTQIELDARETALHEK----MMTLARKERATND 382
Cdd:TIGR02168  891 llrsELEELSEELRELESKRSELRRELEELREKLA-----QLELRLEGLEVRIDNLQERLSEEysltLEEAEALENKIED 965

                          250
                   ....*....|....*....
gi 15234086    383 EYQDARKEMIKVWKANEEL 401
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKEL 984
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 189-317 3.49e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.59  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   189 QQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEK---------NMQEFYQQVLgghEKSFAELEAK-REKL-DERARLIE 257
Cdd:pfam07111 527 QQLEQELQRAQESLASVGQQLEVARQGQQESTEEaaslrqeltQQQEIYGQAL---QEKVAEVETRlREQLsDTKRRLNE 603

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234086   258 QRaikneEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEK-EKLHKRIMEMEAKLN 317
Cdd:pfam07111 604 AR-----REQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEgQRLARRVQELERDKN 659
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
237-400 3.14e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  237 KSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKL 316
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  317 netQELELEIEKLKGTTNVMKHMVGCDGDkdiVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDARKEMIKVWK 396
Cdd:PRK02224 582 ---AELKERIESLERIRTLLAAIADAEDE---IERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK 655


                 ....
gi 15234086  397 ANEE 400
Cdd:PRK02224 656 ERAE 659
 
Name Accession Description Interval E-value
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 29-141 3.13e-49

XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins including gene X and SGS3. SGS3 is thought to be involved in post-transcriptional gene silencing (PTGS). This domain contains a conserved aspartate residue that may be functionally important. The XS domain has recently been predicted to possess an RRM-like RNA-binding domain by fold recognition.


Pssm-ID: 460933  Cd Length: 113  Bit Score: 165.81  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    29 QKRYVWPWVGLVANVPTEVEPSGRRVGKSGSTLRDEFtlKGFNPTRVKPIWNTKGHTGFALVEFAKDFKGFESAMQFEKS 108
Cdd:pfam03468   1 DELFVWPWMGIVVNIPTEQDEDGRWVGMSGEELKDKL--SRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKH 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15234086   109 FDLDRHGKRDW-KKGHRLRDDKLYGWLAREDDYN 141
Cdd:pfam03468  79 FEAQGHGKKDWgGKRNRGSGSKLYGWVARADDYN 112
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 32-140 4.09e-49

RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important.


Pssm-ID: 409710  Cd Length: 107  Bit Score: 165.22  E-value: 4.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  32 YVWPWVGLVANVPTEVEPSGRRVGKSGSTLRDEftLKGFNPTRVKPIWNTKGHTGFALVEFAKDFKGFESAMQFEKSFDL 111
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDNRKMEGGSNKELLER--LIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEV 78

                        90       100
                ....*....|....*....|....*....
gi 15234086 112 DRHGKRDWKKGHRLRDDKLYGWLAREDDY 140
Cdd:cd12266  79 DGHGKKDWRNKKGGRKSKLYGWLARADDY 107
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 410-550 1.14e-45

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 156.98  E-value: 1.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   410 KIMGELNPAPFLPAVMNKH-------KAMMLCSVWAAEIGDVQWTPFRVDESDGTPKQklhisqhskcemqrVVDENDEK 482
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFsneeaevKAAELCSLWEEELKDPEWHPFKVVMVDGKHKE--------------VIDEDDEK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234086   483 LRMLKNQYGEEVYSEVVRAKLEMEEHNASGSYETEELWNYEENRKATIEEITDVMLKirsKLAAMKNK 550
Cdd:pfam03469  67 LKELKEEYGEEVYNAVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILK---QWKALKRK 131
COG5022 COG5022
Myosin heavy chain [General function prediction only];
178-403 1.01e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  178 CQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEKNMQEfyqqvlggheksfaELEAKREKLDERARLIE 257
Cdd:COG5022  873 SAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIE--------------NLEFKTELIARLKKLLN 938

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  258 QRAIKNEEEMEKTRLEREM-IQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQELELEIEKLKGTTNVM 336
Cdd:COG5022  939 NIDLEEGPSIEYVKLPELNkLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL 1018

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234086  337 KHMVGCDGDKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDA--RKEMIKVWKANEELMK 403
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALklRRENSLLDDKQLYQLE 1087
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-406 2.68e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 151 KKKRDLKSISQIVEEDQRKLYHLFENMCQTIEKNKQRKQQLEQKVDETLESLefhnlmlnNSYQEEIQKMEKNmQEFYQQ 230
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------YELLAELARLEQD-IARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 231 VLGGHEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIM 310
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 311 EMEAKLNETQELELEIEKLKgttnvmkhmvgcDGDKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDARKE 390
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE------------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                       250
                ....*....|....*.
gi 15234086 391 MIKVWKANEELMKQEK 406
Cdd:COG1196 458 EEALLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-401 4.58e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    151 KKKRDLKSISQIVEEDQRKLYHLFENMCQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNsYQEEIQKMEKNMQEFyQQ 230
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-LKEELKALREALDEL-RA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    231 VLGGHEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIM 310
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    311 ----EMEAKLNETQELELEIEKLKGTTNVMKHMVGcdgdkDIVEKIAKTQIELDARETALHEK----MMTLARKERATND 382
Cdd:TIGR02168  891 llrsELEELSEELRELESKRSELRRELEELREKLA-----QLELRLEGLEVRIDNLQERLSEEysltLEEAEALENKIED 965

                          250
                   ....*....|....*....
gi 15234086    383 EYQDARKEMIKVWKANEEL 401
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 152-330 7.01e-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: 45.83  E-value: 7.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    152 KKRDLKSISQIVEEDQRKLYHLfenmcqtiEKNKQRKQQLEQKVDETLESLEFHNLMlnnsyqEEIQKMEKNMQEFYQQV 231
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKEL--------EARIEELEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLEEEV 807

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    232 lGGHEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQ-------KEKEK 304
Cdd:TIGR02169  808 -SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdleSRLGD 886

                          170       180       190
                   ....*....|....*....|....*....|
gi 15234086    305 LHKRIMEMEAKLNETQ----ELELEIEKLK 330
Cdd:TIGR02169  887 LKKERDELEAQLRELErkieELEAQIEKKR 916
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 189-317 3.49e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.59  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   189 QQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEK---------NMQEFYQQVLgghEKSFAELEAK-REKL-DERARLIE 257
Cdd:pfam07111 527 QQLEQELQRAQESLASVGQQLEVARQGQQESTEEaaslrqeltQQQEIYGQAL---QEKVAEVETRlREQLsDTKRRLNE 603

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234086   258 QRaikneEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEK-EKLHKRIMEMEAKLN 317
Cdd:pfam07111 604 AR-----REQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEgQRLARRVQELERDKN 659
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-383 3.79e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    179 QTIEKNKQRKQQLEQKVDETLESLEFHNLmlnnsyqeEIQKMEKNMQEfYQQVLGGHEKSFAELEAKREKLDERARLIEQ 258
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRL--------EVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    259 RAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQE-----------LELEIE 327
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqLELQIA 396

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 15234086    328 KLKGTTNVMKHMVgcdgdKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDE 383
Cdd:TIGR02168  397 SLNNEIERLEARL-----ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 150-400 5.74e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   150 VKKKRDLKSISQivEEDQRKLyhlfenmcqtiEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQEEIQK------MEKN 223
Cdd:pfam17380 344 MERERELERIRQ--EERKREL-----------ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAarkvkiLEEE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   224 MQEFYQQVLGGHEKSFAELEAKREKldERARLIEQRAikneEEMEKTRLEREMIQKAMCEQNEANEEAMKlaEKHQKEKE 303
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERA----REMERVRLEEQERQQQVERLRQQEEERKR--KKLELEKE 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   304 KLHKRIMEMEAKLNETQELELEIEKlkgttnvmkhMVGCDGDKDIVEKiaktqiELDARETALH-EKMMTLARKERATND 382
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQA----------MIEEERKRKLLEK------EMEERQKAIYeEERRREAEEERRKQQ 546

                         250
                  ....*....|....*...
gi 15234086   383 EYQDARKEMIKVWKANEE 400
Cdd:pfam17380 547 EMEERRRIQEQMRKATEE 564
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 178-411 1.10e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    178 CQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQEEIQKMEKNMQEfYQQVLGGHEKSFAELEAKREKLDERARLIE 257
Cdd:TIGR00618  530 MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLTEKLSEAED 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    258 QRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIME------------MEAKLNETQELELE 325
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsirvlpkelLASRQLALQKMQSE 688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    326 IEKLKGTTNVMKHMVgcDGDKDIVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDARKEMIKVWKANEELMKQE 405
Cdd:TIGR00618  689 KEQLTYWKEMLAQCQ--TLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN 766


                   ....*.
gi 15234086    406 KIRVKI 411
Cdd:TIGR00618  767 NEEVTA 772
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 163-330 2.22e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 163 VEEDQRKLYHLfenmcQTIEKNKQRKQQLEQKVDETLESLEfhnlmlnnsyqEEIQKMEKNMQEFyQQVLGGHEKSFAEL 242
Cdd:COG1579   2 MPEDLRALLDL-----QELDSELDRLEHRLKELPAELAELE-----------DELAALEARLEAA-KTELEDLEKEIKRL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 243 EAKREKLDERARLIEQR--AIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNE-T 319
Cdd:COG1579  65 ELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkK 144

                       170
                ....*....|.
gi 15234086 320 QELELEIEKLK 330
Cdd:COG1579 145 AELDEELAELE 155
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-406 2.28e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    240 AELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNET 319
Cdd:TIGR02169  688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    320 QELELEIEKLKGTTNVMKHMVGCDGDKDIVEKIAKTQ----------IELDARETALHEKmMTLARKERATNDEYQDARK 389
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEeevsriearlREIEQKLNRLTLE-KEYLEKEIQELQEQRIDLK 846

                          170
                   ....*....|....*..
gi 15234086    390 EMIKVWKANEELMKQEK 406
Cdd:TIGR02169  847 EQIKSIEKEIENLNGKK 863
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
237-400 3.14e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  237 KSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKL 316
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086  317 netQELELEIEKLKGTTNVMKHMVGCDGDkdiVEKIAKTQIELDARETALHEKMMTLARKERATNDEYQDARKEMIKVWK 396
Cdd:PRK02224 582 ---AELKERIESLERIRTLLAAIADAEDE---IERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK 655


                 ....
gi 15234086  397 ANEE 400
Cdd:PRK02224 656 ERAE 659
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-327 3.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 179 QTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSyQEEIQKMEKNMQEFYQQVLGgHEKSFAELEAKREKLDERARLIEQ 258
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLE 414

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234086 259 RAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQELELEIE 327
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-408 3.96e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 202 LEFHNLMLNNSYQEEIQKMEKNMQEFYQQVLGGHEKSFAELEAKREKLDERARLIEQRAiKNEEEMEKTRLEREMIQK-- 279
Cdd:COG4717  40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREel 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 280 AMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAKLNETQELELEIEKLKgtTNVMKHMVGCDGDKDIVEKIAKTQIEL 359
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE--AELAELQEELEELLEQLSLATEEELQD 196

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15234086 360 DARE-TALHEKMMTLARKERATNDEYQDARKEMIKVWKANEELMKQEKIR 408
Cdd:COG4717 197 LAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 148-332 5.76e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   148 KNVKKKRDLKSISQIVEEDQRKLYHL-------FENMCQTIEKNKQRKQQLE------QKVDETLESLEFHNLMLNNSYQ 214
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLeektklqDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKTIC 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086   215 EEIQKMEKNMQEFyQQVLGGHEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEremIQKAMCEQneanEEAMKL 294
Cdd:pfam05483 328 QLTEEKEAQMEEL-NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---LQKKSSEL----EEMTKF 399

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15234086   295 AEKHQKEKEKLHKRIMEMEAKLNETQELELEIEKLKGT 332
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-400 7.54e-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: 39.27  E-value: 7.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    156 LKSISQIVEEDQRKLYHLFENMCQTIEKNKQRKQQLEQKVDETLESLEFHNLMLNNSYQE-EIQKMEKNMQEFYQQVLgg 234
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKlDELAEELAELEEKLEEL-- 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    235 hEKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKAMCEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEA 314
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086    315 KLNETQ--ELELEIEKLKgttnvmkhmvgcdgdkdivEKIAKTQIELDARETALHEKMMTLARKERATNDEYQD-----A 387
Cdd:TIGR02168  429 KLEEAElkELQAELEELE-------------------EELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqA 489

                          250
                   ....*....|...
gi 15234086    388 RKEMIKVWKANEE 400
Cdd:TIGR02168  490 RLDSLERLQENLE 502
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 236-404 8.31e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 236 EKSFAELEAKREKLDERARLIEQRAIKNEEEMEKTRLEREMIQKamcEQNEANEEAMKLAEKHQKEKEKLHKRIMEMEAK 315
Cdd:COG3883  22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234086 316 LNETQELEL-----EIEKLKGTTNVMKHMVgcDGDKDIVEKIAKTQIELDARETALHEKMMTLARKEratnDEYQDARKE 390
Cdd:COG3883  99 GGSVSYLDVllgseSFSDFLDRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALK----AELEAAKAE 172

                       170
                ....*....|....
gi 15234086 391 MIKVWKANEELMKQ 404
Cdd:COG3883 173 LEAQQAEQEALLAQ 186
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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