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Conserved domains on  [gi|1063737361|ref|NP_001331717|]
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Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 402-546 7.72e-88

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


:

Pssm-ID: 465579  Cd Length: 139  Bit Score: 273.65  E-value: 7.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 402 HSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADgcakySNLSAVVTIGFVKDAKHhVDVQGF 481
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG-----KEVVVITTIGFLKEAPH-INVHGF 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737361 482 NVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYW 546
Cdd:pfam17942  75 NVYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase super family cl00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 159-283 1.07e-43

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


The actual alignment was detected with superfamily member cd16931:

Pssm-ID: 469604 [Multi-domain]  Cd Length: 118  Bit Score: 153.72  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 159 FLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMiqNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAK-SKLAD 237
Cdd:cd16931     1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDI--NLLRGGFMLSFLDDGNGMTPEEAHHMISFGFSDKrSDDHD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063737361 238 TIGQYGNGFKTSTMRLGADVIVFSRclgkdgKSSTQSIGLLSYTFL 283
Cdd:cd16931    79 HIGRYGNGFKSGSMRLGRDVIVFTK------KDESQSCGLLSQTFL 118
Myosin_tail_1 super family cl37647
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 705-802 1.25e-06

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.


The actual alignment was detected with superfamily member pfam01576:

Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.10  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  705 LSQLEQENNELRERLDKKEEVflllqkdlrrerelRKTLEAEVETLKNKLKEMDK---EQASLIDVFAEDRDRRDKEEEN 781
Cdd:pfam01576  491 LRQLEDERNSLQEQLEEEEEA--------------KRNVERQLSTLQAQLSDMKKkleEDAGTLEALEEGKKRLQRELEA 556

                           90       100
                   ....*....|....*....|.
gi 1063737361  782 LRIKLEEASNTIQKLIDGKAR 802
Cdd:pfam01576  557 LTQQLEEKAAAYDKLEKTKNR 577
 
Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 402-546 7.72e-88

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


Pssm-ID: 465579  Cd Length: 139  Bit Score: 273.65  E-value: 7.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 402 HSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADgcakySNLSAVVTIGFVKDAKHhVDVQGF 481
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG-----KEVVVITTIGFLKEAPH-INVHGF 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737361 482 NVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYW 546
Cdd:pfam17942  75 NVYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 159-283 1.07e-43

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 153.72  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 159 FLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMiqNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAK-SKLAD 237
Cdd:cd16931     1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDI--NLLRGGFMLSFLDDGNGMTPEEAHHMISFGFSDKrSDDHD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063737361 238 TIGQYGNGFKTSTMRLGADVIVFSRclgkdgKSSTQSIGLLSYTFL 283
Cdd:cd16931    79 HIGRYGNGFKSGSMRLGRDVIVFTK------KDESQSCGLLSQTFL 118
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 172-300 4.40e-20

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 87.00  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 172 GAFAELLDNALDevrSGATFVNVDMIQNRKDGsKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLAD--TIGQYGNGFKTS 249
Cdd:pfam13589   3 GALAELIDNSID---ADATNIKIEVNKNRGGG-TEIVIEDDGHGMSPEELINALRLATSAKEAKRGstDLGRYGIGLKLA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063737361 250 TMRLGADVIVFSRclgKDGKSSTQSiglLSYTFLKStgKEDIVVPMLDYER 300
Cdd:pfam13589  79 SLSLGAKLTVTSK---KEGKSSTLT---LDRDKISN--ENDWLLPLLTPAP 121
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 705-802 1.25e-06

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: 52.10  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  705 LSQLEQENNELRERLDKKEEVflllqkdlrrerelRKTLEAEVETLKNKLKEMDK---EQASLIDVFAEDRDRRDKEEEN 781
Cdd:pfam01576  491 LRQLEDERNSLQEQLEEEEEA--------------KRNVERQLSTLQAQLSDMKKkleEDAGTLEALEEGKKRLQRELEA 556

                           90       100
                   ....*....|....*....|.
gi 1063737361  782 LRIKLEEASNTIQKLIDGKAR 802
Cdd:pfam01576  557 LTQQLEEKAAAYDKLEKTKNR 577
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
705-796 3.05e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDRRDKEEEN 781
Cdd:COG4372    75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLeaqIAELQSEIAEREEELKE 154

                          90
                  ....*....|....*
gi 1063737361 782 LRIKLEEASNTIQKL 796
Cdd:COG4372   155 LEEQLESLQEELAAL 169
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
176-237 6.00e-05

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 46.58  E-value: 6.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737361 176 ELLDNALDevrSGATFVNVDmIQNrkDGSKMILIEDNGGGMNPEKM-----RHcmslgysAKSKLAD 237
Cdd:COG0323    30 ELVENAID---AGATRIEVE-IEE--GGKSLIRVTDNGCGMSPEDLplafeRH-------ATSKIRS 83
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 703-798 8.14e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDRRDKEE 779
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEI 428

                          90
                  ....*....|....*....
gi 1063737361 780 ENLRIKLEEASNTIQKLID 798
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTN 447
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 707-793 3.56e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  707 QLEQENNELRERLDKKEEVFLLLQKDLRRERELRKtlEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEEN-LRIK 785
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQkILDK 99


                   ....*...
gi 1063737361  786 LEEASNTI 793
Cdd:smart00935 100 INKAIKEV 107
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
705-802 4.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAevetLKNKLKEMDKEQASLIDVFaEDRDRRDKEEENLRI 784
Cdd:PRK03918  520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKEL-EELGFESVEELEERL 594

                          90
                  ....*....|....*....
gi 1063737361 785 K-LEEASNTIQKLIDGKAR 802
Cdd:PRK03918  595 KeLEPFYNEYLELKDAEKE 613
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 173-246 4.74e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 37.63  E-value: 4.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737361  173 AFAELLDNALDEVRSGATfVNVDMIQNRKDGSkmILIEDNGGGMNPEKMRHCMSLGYSAKSKlADTIGQYGNGF 246
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGR-ITVTLERDGDHVE--ITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGL 78
 
Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 402-546 7.72e-88

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


Pssm-ID: 465579  Cd Length: 139  Bit Score: 273.65  E-value: 7.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 402 HSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADgcakySNLSAVVTIGFVKDAKHhVDVQGF 481
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG-----KEVVVITTIGFLKEAPH-INVHGF 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063737361 482 NVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYW 546
Cdd:pfam17942  75 NVYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 159-283 1.07e-43

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 153.72  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 159 FLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMiqNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAK-SKLAD 237
Cdd:cd16931     1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDI--NLLRGGFMLSFLDDGNGMTPEEAHHMISFGFSDKrSDDHD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063737361 238 TIGQYGNGFKTSTMRLGADVIVFSRclgkdgKSSTQSIGLLSYTFL 283
Cdd:cd16931    79 HIGRYGNGFKSGSMRLGRDVIVFTK------KDESQSCGLLSQTFL 118
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 172-300 4.40e-20

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 87.00  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 172 GAFAELLDNALDevrSGATFVNVDMIQNRKDGsKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLAD--TIGQYGNGFKTS 249
Cdd:pfam13589   3 GALAELIDNSID---ADATNIKIEVNKNRGGG-TEIVIEDDGHGMSPEELINALRLATSAKEAKRGstDLGRYGIGLKLA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063737361 250 TMRLGADVIVFSRclgKDGKSSTQSiglLSYTFLKStgKEDIVVPMLDYER 300
Cdd:pfam13589  79 SLSLGAKLTVTSK---KEGKSSTLT---LDRDKISN--ENDWLLPLLTPAP 121
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 705-802 1.25e-06

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: 52.10  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  705 LSQLEQENNELRERLDKKEEVflllqkdlrrerelRKTLEAEVETLKNKLKEMDK---EQASLIDVFAEDRDRRDKEEEN 781
Cdd:pfam01576  491 LRQLEDERNSLQEQLEEEEEA--------------KRNVERQLSTLQAQLSDMKKkleEDAGTLEALEEGKKRLQRELEA 556

                           90       100
                   ....*....|....*....|.
gi 1063737361  782 LRIKLEEASNTIQKLIDGKAR 802
Cdd:pfam01576  557 LTQQLEEKAAAYDKLEKTKNR 577
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 709-802 2.86e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.14  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 709 EQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDV---FAEDRDRRDKEEENLRIK 785
Cdd:pfam20492   5 EREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEkerLEESAEMEAEEKEQLEAE 84

                          90
                  ....*....|....*..
gi 1063737361 786 LEEASNTIQKLIDGKAR 802
Cdd:pfam20492  85 LAEAQEEIARLEEEVER 101
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
705-796 3.05e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDRRDKEEEN 781
Cdd:COG4372    75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLeaqIAELQSEIAEREEELKE 154

                          90
                  ....*....|....*
gi 1063737361 782 LRIKLEEASNTIQKL 796
Cdd:COG4372   155 LEEQLESLQEELAAL 169
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 176-237 3.29e-05

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 45.51  E-value: 3.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737361 176 ELLDNALDevrSGATFVNVDMiqnRKDGSKMILIEDNGGGMNPEKM-----RHcmslgysAKSKLAD 237
Cdd:cd16926    20 ELVENSID---AGATRIDVEI---EEGGLKLIRVTDNGSGISREDLelafeRH-------ATSKISS 73
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 703-802 4.12e-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: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDV---FAEDRDRRDKEE 779
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleeLAEELLEALRAA 395

                          90       100
                  ....*....|....*....|...
gi 1063737361 780 ENLRIKLEEASNTIQKLIDGKAR 802
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLER 418
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 703-799 4.54e-05

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: 45.69  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDK------------------KEEVFLLLQKDLRRERELRktLEAEVETLKNKLKEMDKEQASL 764
Cdd:COG1579    59 KEIKRLELEIEEVEARIKKyeeqlgnvrnnkeyealqKEIESLKRRISDLEDEILE--LMERIEELEEELAELEAELAEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063737361 765 IDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDG 799
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEELEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
681-789 5.53e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 681 PERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRREREL---------RKTLEAEVETLK 751
Cdd:COG4717    66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqllplyqeLEALEAELAELP 145

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063737361 752 NKLKEMDKEQASLIDVfAEDRDRRDKEEENLRIKLEEA 789
Cdd:COG4717   146 ERLEELEERLEELREL-EEELEELEAELAELQEELEEL 182
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
176-237 6.00e-05

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 46.58  E-value: 6.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063737361 176 ELLDNALDevrSGATFVNVDmIQNrkDGSKMILIEDNGGGMNPEKM-----RHcmslgysAKSKLAD 237
Cdd:COG0323    30 ELVENAID---AGATRIEVE-IEE--GGKSLIRVTDNGCGMSPEDLplafeRH-------ATSKIRS 83
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 705-804 7.17e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEvfllLQKDLRRERELRKTLEAEVEtLKNKLKEMDKEQA-----SLIDVFAEDRDRRDKEE 779
Cdd:pfam13868 207 RAKLYQEEQERKERQKEREE----AEKKARQRQELQQAREEQIE-LKERRLAEEAEREeeefeRMLRKQAEDEEIEQEEA 281

                          90       100
                  ....*....|....*....|....*
gi 1063737361 780 ENLRIKLEEASNTIQKLIDGKARGR 804
Cdd:pfam13868 282 EKRRMKRLEHRRELEKQIEEREEQR 306
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 173-262 8.57e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 42.36  E-value: 8.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 173 AFAELLDNALDEVRSGAT-FVNVdmiqnRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSaksklADTIGQYGNGF----- 246
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEiTVTL-----SEGGELTLTVEDNGIGIPPEDLPRIFEPFST-----ADKRGGGGTGLglsiv 78

                          90
                  ....*....|....*.
gi 1063737361 247 KTSTMRLGADVIVFSR 262
Cdd:pfam02518  79 RKLVELLGGTITVESE 94
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 705-796 2.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRI 784
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                          90
                  ....*....|..
gi 1063737361 785 KLEEASNTIQKL 796
Cdd:COG1196   391 ALRAAAELAAQL 402
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 705-789 2.74e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEA---EVETLKNKLKEM----DKEQASL----------IDV 767
Cdd:pfam20492  15 LKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQkrqEAEEEKERLEESaemeAEEKEQLeaelaeaqeeIAR 94

                          90       100
                  ....*....|....*....|..
gi 1063737361 768 FAEDRDRRDKEEENLRIKLEEA 789
Cdd:pfam20492  95 LEEEVERKEEEARRLQEELEEA 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 705-798 3.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKK-EEVFLL------LQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDK 777
Cdd:COG1196   269 LEELRLELEELELELEEAqAEEYELlaelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                          90       100
                  ....*....|....*....|.
gi 1063737361 778 EEENLRIKLEEASNTIQKLID 798
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLE 369
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
729-796 4.51e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 729 LQKDLRRERELRKT---LEAEVETLKNKLKEMDKEQASLIDVFAEDRD-------------RRDKEEENLRIKLEEASNT 792
Cdd:COG2433   408 LTEEEEEIRRLEEQverLEAEVEELEAELEEKDERIERLERELSEARSeerreirkdreisRLDREIERLERELEEERER 487


                  ....
gi 1063737361 793 IQKL 796
Cdd:COG2433   488 IEEL 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 705-802 4.90e-04

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: 43.21  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRI 784
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220

                          90
                  ....*....|....*...
gi 1063737361 785 KLEEASNTIQKLIDGKAR 802
Cdd:COG4942   221 EAEELEALIARLEAEAAA 238
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 700-796 5.64e-04

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: 42.22  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 700 SGPRTLSQLEQENNELRERLDKKEEVFlllqKDLRRERelrKTLEAEVETLKNKLKEMDKEQASL------------IDV 767
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTEL----EDLEKEI---KRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeIES 100

                          90       100
                  ....*....|....*....|....*....
gi 1063737361 768 FAEDRDRRDKEEENLRIKLEEASNTIQKL 796
Cdd:COG1579   101 LKRRISDLEDEILELMERIEELEEELAEL 129
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 703-798 8.14e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDRRDKEE 779
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqIKKLQQEKELLEKEI 428

                          90
                  ....*....|....*....
gi 1063737361 780 ENLRIKLEEASNTIQKLID 798
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTN 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 703-798 8.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENL 782
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                          90
                  ....*....|....*.
gi 1063737361 783 RIKLEEASNTIQKLID 798
Cdd:COG1196   375 AEAEEELEELAEELLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 703-802 9.52e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENL 782
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100
                  ....*....|....*....|
gi 1063737361 783 RIKLEEASNTIQKLIDGKAR 802
Cdd:COG1196   382 EELAEELLEALRAAAELAAQ 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
687-796 1.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 687 ELPGKSSELPKPQSGPRT--LSQLEQENNELRERLDKKEEvFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQAsL 764
Cdd:COG4717    50 RLEKEADELFKPQGRKPElnLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLLQ-L 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063737361 765 IDVFAEDRD----------------RRDKEEENLRIKLEEASNTIQKL 796
Cdd:COG4717   128 LPLYQELEAleaelaelperleeleERLEELRELEEELEELEAELAEL 175
Cep57_CLD_2 pfam14197
Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle ...
 708-757 1.35e-03

Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle pole body protein PPC89 has low similarity to the human Cep57 protein. The CLD or centrosome localization domain of Cep57 and PPC89 is found at the N-terminus. This region localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57 and PPC89.


Pssm-ID: 372959 [Multi-domain]  Cd Length: 67  Bit Score: 37.65  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737361 708 LEQENNELRERLD---KKEEVFLLLQKDLRRERE--LRK---------TLEAEVETLKNKLKEM 757
Cdd:pfam14197   1 LEAENLTLQNRLDsltRKVAVHEIELKRLRRERDsaVRQlgvayleiqELKAENEALRKELKEQ 64
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 174-234 1.45e-03

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 41.76  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737361 174 FAELLDNALDEVRSGAT---FVNVDMIQNrkDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSK 234
Cdd:COG3290   286 LGNLLDNAIEAVEKLPEeerRVELSIRDD--GDELVIEVEDSGPGIPEELLEKIFERGFSTKLG 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 707-796 2.63e-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: 41.59  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  707 QLEQENNELRERLDKKEEvflllQKDLRRERElrKTLEAEVETLKNKLKEMDKEQASLIDVFAE---DRDRRDKEEENLR 783
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKE-----QIKSIEKEI--ENLNGKKEELEEELEELEAALRDLESRLGDlkkERDELEAQLRELE 902

                           90
                   ....*....|...
gi 1063737361  784 IKLEEASNTIQKL 796
Cdd:TIGR02169  903 RKIEELEAQIEKK 915
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 703-799 3.05e-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: 41.20  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENL 782
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339

                           90
                   ....*....|....*..
gi 1063737361  783 RiKLEEASNTIQKLIDG 799
Cdd:TIGR02168  340 A-ELEEKLEELKEELES 355
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
703-796 3.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENL 782
Cdd:COG4717   132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211

                          90
                  ....*....|....
gi 1063737361 783 RIKLEEASNTIQKL 796
Cdd:COG4717   212 EEELEEAQEELEEL 225
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 703-783 3.29e-03

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: 39.50  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELR---KTLEAEVETLKNKLKEMDKEQASLIDVFA---EDRDR-R 775
Cdd:pfam13851  47 KLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqslKNLKARLKVLEKELKDLKWEHEVLEQRFEkveRERDElY 126


                  ....*...
gi 1063737361 776 DKEEENLR 783
Cdd:pfam13851 127 DKFEAAIQ 134
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 707-793 3.56e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  707 QLEQENNELRERLDKKEEVFLLLQKDLRRERELRKtlEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEEN-LRIK 785
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQkILDK 99


                   ....*...
gi 1063737361  786 LEEASNTI 793
Cdd:smart00935 100 INKAIKEV 107
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 173-220 3.75e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 37.77  E-value: 3.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1063737361 173 AFAELLDNALDEVRSGAtfvNVDMIQNRKDGSKMIlIEDNGGGMNPEK 220
Cdd:cd16940    17 LLRNLVDNAVRYSPQGS---RVEIKLSADDGAVIR-VEDNGPGIDEEE 60
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
705-802 4.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAevetLKNKLKEMDKEQASLIDVFaEDRDRRDKEEENLRI 784
Cdd:PRK03918  520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKEL-EELGFESVEELEERL 594

                          90
                  ....*....|....*....
gi 1063737361 785 K-LEEASNTIQKLIDGKAR 802
Cdd:PRK03918  595 KeLEPFYNEYLELKDAEKE 613
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 705-793 4.40e-03

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 39.03  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRER--LDK-KEEVFLLLQKD---LRRERELrktLEAEVETLKNKLK-EMDKEQASLIDVFAEDRDRRDK 777
Cdd:pfam07798  43 VTKEDLENETYLQKadLAElRSELQILEKSEfaaLRSENEK---LRRELEKLKQRLReEITKLKADVRLDLNLEKGRIRE 119

                          90
                  ....*....|....*.
gi 1063737361 778 EEENLRIKLEEASNTI 793
Cdd:pfam07798 120 ELKAQELKIQETNNKI 135
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 703-762 4.53e-03

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 39.81  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFL--LLQK----------------DLRRER-ELRKTLEAEVETLKNKL-KEMDKEQA 762
Cdd:pfam09755 114 RKLTQLRQEKVELEQTLEQEQEYQVnkLMRKiekleaetlnkqtnleQLRREKvELENTLEQEQEALVNRLwKRMDKLEA 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 714-802 4.71e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 714 ELRERLDKKEEVFLLLQKDLRRERelRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDRRDKEEENLRIKLEEAS 790
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAE--LEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELL 294

                          90
                  ....*....|..
gi 1063737361 791 NTIQKLIDGKAR 802
Cdd:COG1196   295 AELARLEQDIAR 306
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 173-246 4.74e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 37.63  E-value: 4.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063737361  173 AFAELLDNALDEVRSGATfVNVDMIQNRKDGSkmILIEDNGGGMNPEKMRHCMSLGYSAKSKlADTIGQYGNGF 246
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGR-ITVTLERDGDHVE--ITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGL 78
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 177-233 5.25e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 37.27  E-value: 5.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063737361 177 LLDNALDEV-RSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKS 233
Cdd:cd16915     8 LIDNALDALaATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKG 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 698-797 5.63e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 698 PQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLidvfAEDRDRRDK 777
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEK 90

                          90       100
                  ....*....|....*....|
gi 1063737361 778 EEENLRIKLEEASNTIQKLI 797
Cdd:COG4942    91 EIAELRAELEAQKEELAELL 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 713-796 5.73e-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: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 713 NELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKE----QASL------IDVFAEDRDRRDKEEENL 782
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaQAEEyellaeLARLEQDIARLEERRREL 314

                          90
                  ....*....|....
gi 1063737361 783 RIKLEEASNTIQKL 796
Cdd:COG1196   315 EERLEELEEELAEL 328
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 705-800 7.06e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.82  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 705 LSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKT-LEAEVETLKNKLKEMDKEQAS---LIDVfaeDRDRRDkeEE 780
Cdd:pfam12795 115 PERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWaLQAELAALKAQIDMLEQELLSnnnRQDL---LKARRD--LL 189

                          90       100
                  ....*....|....*....|.
gi 1063737361 781 NLRI-KLEEASNTIQKLIDGK 800
Cdd:pfam12795 190 TLRIqRLEQQLQALQELLNEK 210
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
703-804 8.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLR-RERELrKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEEN 781
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAeREEEL-KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                          90       100
                  ....*....|....*....|...
gi 1063737361 782 LRIKLEEASNTIQKLIDGKARGR 804
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPREL 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 705-796 9.03e-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: 39.65  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  705 LSQLEQENNELRERLDKKEEVFLLLQKDLRR-------ERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDK 777
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEElsrqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90
                   ....*....|....*....
gi 1063737361  778 EEEnlriKLEEASNTIQKL 796
Cdd:TIGR02168  773 AEE----ELAEAEAEIEEL 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 703-802 9.41e-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: 39.67  E-value: 9.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361  703 RTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDR---RDKEE 779
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdYREKL 394

                           90       100
                   ....*....|....*....|...
gi 1063737361  780 ENLRIKLEEASNTIQKLIDGKAR 802
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQR 417
Filament pfam00038
Intermediate filament protein;
707-798 9.56e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.13  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063737361 707 QLEQENNELRERLDkkeevfLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASL---IDVFAEDRDR---RDKEEE 780
Cdd:pfam00038  22 FLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLqleLDNLRLAAEDfrqKYEDEL 95

                          90
                  ....*....|....*...
gi 1063737361 781 NLRIKLEEASNTIQKLID 798
Cdd:pfam00038  96 NLRTSAENDLVGLRKDLD 113
 
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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