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Conserved domains on  [gi|528501420|ref|XP_005157489|]
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huntingtin-interacting protein 1 isoform X1 [Danio rerio]

Protein Classification

ANTH domain-containing protein( domain architecture ID 13730376)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to Caenorhabditis elegans huntington interacting protein related 1 that regulates pre-synaptic vesicle recycling at neuromuscular junctions of mechanosensory neurons

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
40-306 2.79e-89

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


:

Pssm-ID: 400137  Cd Length: 272  Bit Score: 287.27  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    40 QAVSINKAINTQEVAVKEKHARTCILGTHH-EKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   119 ADLNDMSRMWGH-LSEGYGKLCSIYLKLLITKMEFHIKNPRFPGNLQMSNRQLDEAGENDVNNFfqLTVEMFDYLECELN 197
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   198 LFLGVFSSLDMSRSVSVTaAGQCRLAPLIQVILDSSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFQEQFKKLKS 271
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 528501420   272 LFYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
836-1034 1.82e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 268.85  E-value: 1.82e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    836 GIKMEVNERILASCTDLMQAIRVLVLSSKDLQRDIVESGRGAASMKEFYAKNSRWTEGLISASKAVGWGATMLVDAADQV 915
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    916 VQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQ-IEDTETMDFSAMT 994
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 528501420    995 LTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYELA 1034
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
483-581 3.04e-33

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


:

Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 123.58  E-value: 3.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   483 HADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 528501420   563 SNEQLGTQLSALVAEKAGL 581
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-825 8.11e-17

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.76  E-value: 8.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQANEQRY-TKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQ 528
Cdd:COG1196   323 EELAELEEELEELEEELEELeEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  529 EKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTN 608
Cdd:COG1196   403 EELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  609 ERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALD 688
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  689 CVERLRSSRDGfvsdntDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMG 768
Cdd:COG1196   562 AIEYLKAAKAG------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420  769 AADCSRLRTALDSVKALGEKLRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEE 825
Cdd:COG1196   636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
40-306 2.79e-89

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 287.27  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    40 QAVSINKAINTQEVAVKEKHARTCILGTHH-EKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   119 ADLNDMSRMWGH-LSEGYGKLCSIYLKLLITKMEFHIKNPRFPGNLQMSNRQLDEAGENDVNNFfqLTVEMFDYLECELN 197
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   198 LFLGVFSSLDMSRSVSVTaAGQCRLAPLIQVILDSSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFQEQFKKLKS 271
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 528501420   272 LFYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
836-1034 1.82e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 268.85  E-value: 1.82e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    836 GIKMEVNERILASCTDLMQAIRVLVLSSKDLQRDIVESGRGAASMKEFYAKNSRWTEGLISASKAVGWGATMLVDAADQV 915
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    916 VQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQ-IEDTETMDFSAMT 994
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 528501420    995 LTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYELA 1034
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
40-153 4.47e-83

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 264.21  E-value: 4.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17013     1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501420  120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17013    81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
886-1032 1.14e-59

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 200.89  E-value: 1.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   886 KNSRWTEGLISASKAVGWGATMLVDAADQVVQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVT 965
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420   966 QATAGVVASTKSGKSQIED--TETMDFSAMTLTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYE 1032
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
40-160 1.59e-35

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 131.21  E-value: 1.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420     40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVIKDSMRH 117
Cdd:smart00273    3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEALRN 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 528501420    118 KADLNDMSRMWGHLSEG--YGKLCSIYLKLLITKMEFHIKNPRFP 160
Cdd:smart00273   83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
483-581 3.04e-33

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 123.58  E-value: 3.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   483 HADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 528501420   563 SNEQLGTQLSALVAEKAGL 581
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-825 8.11e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.76  E-value: 8.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQANEQRY-TKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQ 528
Cdd:COG1196   323 EELAELEEELEELEEELEELeEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  529 EKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTN 608
Cdd:COG1196   403 EELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  609 ERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALD 688
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  689 CVERLRSSRDGfvsdntDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMG 768
Cdd:COG1196   562 AIEYLKAAKAG------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420  769 AADCSRLRTALDSVKALGEKLRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEE 825
Cdd:COG1196   636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
376-1032 1.45e-15

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: 82.03  E-value: 1.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   376 RLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQAlgesEFLRAELDDLRRVKEDTEKEqrsL 455
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----QILRERLANLERQLEELEAQ---L 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   456 SEIERKAQANEQRYTKLKEKYTELVQSHADLlrknaevtrqmtvaRAAQDEVENVKKEMQDRLKVAQDSASQQEKAQ--- 532
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESL--------------EAELEELEAELEELESRLEELEEQLETLRSKVaql 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   533 LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSAlvAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERES 612
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   613 GVKAAEALQ---NQLNEKESREQALES--ELVSLRWASLRAALEEAGKI------VQDSLN---QLEDPAHISCTSSADY 678
Cdd:TIGR02168  470 LEEAEQALDaaeRELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLsgilgvLSELISvdeGYEAAIEAALGGRLQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   679 LVSR-CQVALDCVERLRSSRDGFVS--DNTDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADS------VKA 749
Cdd:TIGR02168  550 VVVEnLNAAKKAIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   750 CGAEALTLLCQLKEQESMGAADcsrlrtaldsvkalGEKLRPRGLELQQGELGDLVEQEmaaTSAAVESAAARIEEMLNK 829
Cdd:TIGR02168  630 DLDNALELAKKLRPGYRIVTLD--------------GDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   830 SRAvdtgIKMEVNErILASCTDLMQAIRVLVLSSKDLQRDIVEsgrGAASMKEFYAKNSRWTEGLISASKAVGWGATMLV 909
Cdd:TIGR02168  693 IAE----LEKALAE-LRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   910 DAADQVVQgkgKFEELMVCSHEIAASTAQlVAASKVKAEKGSSNLSRLQQAsKGVTQATAGVVASTKSG-KSQIEDTETM 988
Cdd:TIGR02168  765 ELEERLEE---AEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESlERRIAATERR 839
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 528501420   989 dfSAMTLTQIKRQEMDAQVLVLELE------TRLQKERERLGELRKKHYE 1032
Cdd:TIGR02168  840 --LEDLEEQIEELSEDIESLAAEIEeleeliEELESELEALLNERASLEE 887
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
378-652 1.33e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.36  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlkqqALGESEFLRAELDDLRRVKEDTEKE----QR 453
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRdeelRD 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  454 SLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAA----QDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:PRK02224  329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedrREEIEELEEEIEELRERFGDAPVDLG 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  530 KAQ--LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQL---------GTQLsalvaEKAGLVETVSRKEVELSGLGAE 598
Cdd:PRK02224  409 NAEdfLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecGQPV-----EGSPHVETIEEDRERVEELEAE 483
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501420  599 LERLQSSlTNERESGVKAAEALQNQLNEKESREQalESELVSLRWASLRAALEE 652
Cdd:PRK02224  484 LEDLEEE-VEEVEERLERAEDLVEAEDRIERLEE--RREDLEELIAERRETIEE 534
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
326-666 2.82e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 61.39  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   326 VVETEDLVDTDI-PPLTGTGDSKFDDLFGTSAATDPFNFNSQNGMRkddkdrliEQLTAELQALKEELESFRLESGRLCQ 404
Cdd:pfam12128  554 VISPELLHRTDLdPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE--------EELRERLDKAEEALQSAREKQAAAEE 625
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   405 ALRGRVNELEAELAEQThLKQQALGESEflraelDDLRRVKEDTEKEQRSLSE--IERKAQANEQRyTKLKEKYTELVQS 482
Cdd:pfam12128  626 QLVQANGELEKASREET-FARTALKNAR------LDLRRLFDEKQSEKDKKNKalAERKDSANERL-NSLEAQLKQLDKK 697
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   483 HADLLRKNAEVTRQMTVAR-AAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSR-----------TEL 550
Cdd:pfam12128  698 HQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkREI 777
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   551 ETLKSTVTSSQQsNEQLGTQL-----SALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNER---ESGVKAAEALQN 622
Cdd:pfam12128  778 RTLERKIERIAV-RRQEVLRYfdwyqETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRaklEMERKASEKQQV 856
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528501420   623 QLNEKESREQALESELVSLRwasLRAALEEAGKIVQDSLNQLED 666
Cdd:pfam12128  857 RLSENLRGLRCEMSKLATLK---EDANSEQAQGSIGERLAQLED 897
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
493-665 1.23e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  493 VTRQMTVARAAQDEVENVKKEMQDRLKVAQD------------SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSS 560
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  561 QQSNE----------------QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNEREsgvKAAEALQNQL 624
Cdd:COG3206   246 RAQLGsgpdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ---RILASLEAEL 322
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528501420  625 NEKESREQALESELvslrwASLRAALEEAGKIVQDsLNQLE 665
Cdd:COG3206   323 EALQAREASLQAQL-----AQLEARLAELPELEAE-LRRLE 357
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
502-658 2.28e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  502 AAQDEVENVKKEMQDRLKVAQDSASQ-QEKAQ--LEQLQALQAELMSSRTELETLKSTVtssqqsNEQLGTQLSALVAEk 578
Cdd:cd22656   107 TDDEELEEAKKTIKALLDDLLKEAKKyQDKAAkvVDKLTDFENQTEKDQTALETLEKAL------KDLLTDEGGAIARK- 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  579 aglvetvsrkevELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWA--SLRAALEEAGKI 656
Cdd:cd22656   180 ------------EIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDldNLLALIGPAIPA 247

                  ..
gi 528501420  657 VQ 658
Cdd:cd22656   248 LE 249
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
40-306 2.79e-89

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 287.27  E-value: 2.79e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    40 QAVSINKAINTQEVAVKEKHARTCILGTHH-EKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   119 ADLNDMSRMWGH-LSEGYGKLCSIYLKLLITKMEFHIKNPRFPGNLQMSNRQLDEAGENDVNNFfqLTVEMFDYLECELN 197
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   198 LFLGVFSSLDMSRSVSVTaAGQCRLAPLIQVILDSSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFQEQFKKLKS 271
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 528501420   272 LFYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
836-1034 1.82e-83

I/LWEQ domain; Thought to possess an F-actin binding function.


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 268.85  E-value: 1.82e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    836 GIKMEVNERILASCTDLMQAIRVLVLSSKDLQRDIVESGRGAASMKEFYAKNSRWTEGLISASKAVGWGATMLVDAADQV 915
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420    916 VQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQ-IEDTETMDFSAMT 994
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 528501420    995 LTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYELA 1034
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
40-153 4.47e-83

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 264.21  E-value: 4.47e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17013     1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501420  120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17013    81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
40-153 4.77e-70

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 228.32  E-value: 4.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17006     1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501420  120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17006    81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
886-1032 1.14e-59

I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.


Pssm-ID: 460265 [Multi-domain]  Cd Length: 149  Bit Score: 200.89  E-value: 1.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   886 KNSRWTEGLISASKAVGWGATMLVDAADQVVQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVT 965
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420   966 QATAGVVASTKSGKSQIED--TETMDFSAMTLTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYE 1032
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
40-153 2.47e-56

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.


Pssm-ID: 340811  Cd Length: 114  Bit Score: 190.08  E-value: 2.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17014     1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 528501420  120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17014    81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
42-153 7.91e-37

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 134.43  E-value: 7.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHP--NVIKDSMRH-K 118
Cdd:cd16986     3 KAVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDAwL 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 528501420  119 ADLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd16986    83 PELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
40-160 1.59e-35

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 131.21  E-value: 1.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420     40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVIKDSMRH 117
Cdd:smart00273    3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEALRN 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 528501420    118 KADLNDMSRMWGHLSEG--YGKLCSIYLKLLITKMEFHIKNPRFP 160
Cdd:smart00273   83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
483-581 3.04e-33

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 123.58  E-value: 3.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   483 HADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 528501420   563 SNEQLGTQLSALVAEKAGL 581
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
42-153 5.93e-28

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 108.93  E-value: 5.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKADL 121
Cdd:cd17007     3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 528501420  122 NDMSRMW-GHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17007    83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-825 8.11e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.76  E-value: 8.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQANEQRY-TKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQ 528
Cdd:COG1196   323 EELAELEEELEELEEELEELeEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  529 EKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTN 608
Cdd:COG1196   403 EELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  609 ERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALD 688
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  689 CVERLRSSRDGfvsdntDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMG 768
Cdd:COG1196   562 AIEYLKAAKAG------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420  769 AADCSRLRTALDSVKALGEKLRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEE 825
Cdd:COG1196   636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
378-653 9.28e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.29  E-value: 9.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEqthLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSE 457
Cdd:COG1196   234 LRELEAELEELEAELEELEAEL----EELEAELAELEAELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  458 IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVEnvkkEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  538 ALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGVKAA 617
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 528501420  618 EALQNQLNEKESREQALESELVSLRWASLRAALEEA 653
Cdd:COG1196   463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
376-1032 1.45e-15

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: 82.03  E-value: 1.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   376 RLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQAlgesEFLRAELDDLRRVKEDTEKEqrsL 455
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----QILRERLANLERQLEELEAQ---L 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   456 SEIERKAQANEQRYTKLKEKYTELVQSHADLlrknaevtrqmtvaRAAQDEVENVKKEMQDRLKVAQDSASQQEKAQ--- 532
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESL--------------EAELEELEAELEELESRLEELEEQLETLRSKVaql 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   533 LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSAlvAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERES 612
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   613 GVKAAEALQ---NQLNEKESREQALES--ELVSLRWASLRAALEEAGKI------VQDSLN---QLEDPAHISCTSSADY 678
Cdd:TIGR02168  470 LEEAEQALDaaeRELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLsgilgvLSELISvdeGYEAAIEAALGGRLQA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   679 LVSR-CQVALDCVERLRSSRDGFVS--DNTDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADS------VKA 749
Cdd:TIGR02168  550 VVVEnLNAAKKAIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVD 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   750 CGAEALTLLCQLKEQESMGAADcsrlrtaldsvkalGEKLRPRGLELQQGELGDLVEQEmaaTSAAVESAAARIEEMLNK 829
Cdd:TIGR02168  630 DLDNALELAKKLRPGYRIVTLD--------------GDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   830 SRAvdtgIKMEVNErILASCTDLMQAIRVLVLSSKDLQRDIVEsgrGAASMKEFYAKNSRWTEGLISASKAVGWGATMLV 909
Cdd:TIGR02168  693 IAE----LEKALAE-LRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   910 DAADQVVQgkgKFEELMVCSHEIAASTAQlVAASKVKAEKGSSNLSRLQQAsKGVTQATAGVVASTKSG-KSQIEDTETM 988
Cdd:TIGR02168  765 ELEERLEE---AEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESlERRIAATERR 839
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 528501420   989 dfSAMTLTQIKRQEMDAQVLVLELE------TRLQKERERLGELRKKHYE 1032
Cdd:TIGR02168  840 --LEDLEEQIEELSEDIESLAAEIEeleeliEELESELEALLNERASLEE 887
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
398-665 3.76e-15

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: 80.49  E-value: 3.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   398 ESGRLCQA-----LRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTkl 472
Cdd:TIGR02168  669 NSSILERRreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-- 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   473 kEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELET 552
Cdd:TIGR02168  747 -ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   553 LKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQS---SLTNERESGVKAAEALQNQLNEKES 629
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleALLNERASLEEALALLRSELEELSE 901
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 528501420   630 REQALESELVslrwaSLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02168  902 ELRELESKRS-----ELRRELEELREKLAQLELRLE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
409-653 1.62e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  409 RVNELEAELAEQ-THLKQQA---------LGESEFLRAEL--DDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKY 476
Cdd:COG1196   190 RLEDILGELERQlEPLERQAekaeryrelKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  477 TELVQSHADLLRKNAEVTRQMTVARAAQDEVEN---VKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETL 553
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  554 KSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQA 633
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
                         250       260
                  ....*....|....*....|
gi 528501420  634 LESELVSLrwASLRAALEEA 653
Cdd:COG1196   430 LAELEEEE--EEEEEALEEA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
378-666 2.88e-13

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: 74.32  E-value: 2.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   378 IEQLTAELQALK---EELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKE----DTEK 450
Cdd:TIGR02168  693 IAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleeRLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   451 EQRSLSEIERKAQANEQRYTKLKEkytELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEK 530
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKE---ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   531 AQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLT--N 608
Cdd:TIGR02168  850 LS-EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420   609 ERESGVKAAEA-LQNQLNEKESREQALESELVSL----------RWASLRAALEEAGKIVQDSLNQLED 666
Cdd:TIGR02168  929 LRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKieddeeearrRLKRLENKIKELGPVNLAAIEEYEE 997
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-826 7.94e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 7.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  530 KAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEkAGLVETVSRKEVELSGLGAELERLQSSLTNE 609
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG-AVAVLIGVEAAYEAALEAALAAALQNIVVED 555
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  610 RESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHiscTSSADYLVSRCQVALDC 689
Cdd:COG1196   556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLVAARL 632
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  690 VERLRSSRdGFVSDNTDVSGLVRAVTQFAHLVGDvIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMGA 769
Cdd:COG1196   633 EAALRRAV-TLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420  770 ADCSRLRTALDSVKALGEK------------LRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEEM 826
Cdd:COG1196   711 EAEEERLEEELEEEALEEQleaereelleelLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-1030 8.98e-12

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: 69.70  E-value: 8.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   366 QNGMRKDDKDRLIEQLTAELQALKEELESFRL---ESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLR 442
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   443 RVKEDTEKEQRSLSEiERKAQANEQRYTKLKEKYTELvqshadllrknAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQ 522
Cdd:TIGR02168  407 ARLERLEDRRERLQQ-EIEELLKKLEEAELKELQAEL-----------EELEEELEELQEELERLEEALEELREELEEAE 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   523 dSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAekagLVETVSRKEVELSGLGAelERL 602
Cdd:TIGR02168  475 -QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE----LISVDEGYEAAIEAALG--GRL 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   603 QSSLTNERESGVKAAEALqnqlnEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDpaHISCTSSA----DY 678
Cdd:TIGR02168  548 QAVVVENLNAAKKAIAFL-----KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKLrkalSY 620
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   679 LVSRCQVA--LDCVERLRSSRDgfvsdntdvsGLVRAVTQFAHLV--GDVIVQGSATSHMVPVEQADALADSVKACgaEA 754
Cdd:TIGR02168  621 LLGGVLVVddLDNALELAKKLR----------PGYRIVTLDGDLVrpGGVITGGSAKTNSSILERRREIEELEEKI--EE 688
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   755 LTLLCQLKEQEsmgaadCSRLRTALDSVKALGEKLRPRGLELQQgeLGDLVEQEMAATSAAVESAAARIEEmLNKSRAVD 834
Cdd:TIGR02168  689 LEEKIAELEKA------LAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   835 TGIKMEVNERILASCTDLMQAIRVLVlsskDLQRDIvesgrgaasmKEFYAKNSRWTEGLISASKAVgwgaTMLVDAADQ 914
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIE----ELEAQI----------EQLKEELKALREALDELRAEL----TLLNEEAAN 821
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   915 VVQGKGKFEELMvcsHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQIEdtetmdfsAMT 994
Cdd:TIGR02168  822 LRERLESLERRI---AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE--------ALA 890
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 528501420   995 LTQIKRQEMDAQvlVLELETRLQKERERLGELRKKH 1030
Cdd:TIGR02168  891 LLRSELEELSEE--LRELESKRSELRRELEELREKL 924
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
404-650 1.16e-10

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: 64.79  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  404 QALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEqrsLSEIERKAQANEQRYTKLKEKYTELVQSH 483
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELEAQKEEL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  484 ADLLRKNAEVTRQ--MTVARAAQDEVENVkkemqdRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQ 561
Cdd:COG4942   107 AELLRALYRLGRQppLALLLSPEDFLDAV------RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  562 QSNEQLGTQLSALVAEKAGLVETVSRKEVELSglgAELERLQssltneresgvKAAEALQNQLNEKESREQALESELVSL 641
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELA---AELAELQ-----------QEAEELEALIARLEAEAAAAAERTPAA 246

                  ....*....
gi 528501420  642 RWASLRAAL 650
Cdd:COG4942   247 GFAALKGKL 255
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
370-618 3.47e-10

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: 64.32  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   370 RKDDKDRLIEQLTAELQALKEELESFRlesgRLCQALRGRVNELEAELAEQThLKQQALGESEFLR---------AELDD 440
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLT----EEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLRvkekigeleAEIAS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   441 LRRVKEDTEKEQRSLSEIERKAQANEQRY------------------TKLKEKYTELVQSHADLLRKNAEVTRQMTVARA 502
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLlaeieelereieeerkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   503 AQD----EVENVKKEM------QDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLS 572
Cdd:TIGR02169  386 ELKdyreKLEKLKREInelkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 528501420   573 ALVAEKAGLVETVSRKEVELSGLGAELERL--QSSLTNERESGVKAAE 618
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGRAVE 513
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
375-666 5.62e-10

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: 63.55  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   375 DRLIEQLTAELQALKEELESFRLesgrLCQALRGRVNELEAELAEQthLKQQALgESEFLRAELDDLRRVKEDTEKEqrs 454
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDL----IIDEKRQQLERLRREREKA--ERYQAL-LKEKREYEGYELLKEKEALERQ--- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQmtVARAAQDEVENVKKEMQDrLKVAQDSASQQEKAQLE 534
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGE-LEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   535 QLQALQAELMSSRTELETLKSTVtssqqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERE--- 611
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEI-------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelk 388
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 528501420   612 SGVKAAEALQNQLNEKESREQALESELVSLRwaSLRAALEEAGKIVQDSLNQLED 666
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLS--EELADLNAAIAGIEAKINELEE 441
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
378-652 1.33e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.36  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlkqqALGESEFLRAELDDLRRVKEDTEKE----QR 453
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRdeelRD 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  454 SLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAA----QDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:PRK02224  329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedrREEIEELEEEIEELRERFGDAPVDLG 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  530 KAQ--LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQL---------GTQLsalvaEKAGLVETVSRKEVELSGLGAE 598
Cdd:PRK02224  409 NAEdfLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecGQPV-----EGSPHVETIEEDRERVEELEAE 483
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501420  599 LERLQSSlTNERESGVKAAEALQNQLNEKESREQalESELVSLRWASLRAALEE 652
Cdd:PRK02224  484 LEDLEEE-VEEVEERLERAEDLVEAEDRIERLEE--RREDLEELIAERRETIEE 534
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
378-663 2.26e-09

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: 61.57  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   378 IEQLTAELQALKEELESFRLE---SGRLCQALRGRVNELEAELAEqthLKQQAlgeseflraELDDLRRVKEDTEKEQRS 454
Cdd:TIGR04523  255 LNQLKDEQNKIKKQLSEKQKEleqNNKKIKELEKQLNQLKSEISD---LNNQK---------EQDWNKELKSELKNQEKK 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvarAAQDEVENVKKEMQDRLKVAQDSASQ------- 527
Cdd:TIGR04523  323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQNEIEKLKKENQSYKQEIKNLESQindlesk 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   528 -----QEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQ---------------------QSNEQLGTQLSALVAE--- 577
Cdd:TIGR04523  400 iqnqeKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKNNseikdltnqdsvkeliiknldNTRESLETQLKVLSRSink 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   578 -KAGLVETV---SRKEVELSGLGAE---LERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAAL 650
Cdd:TIGR04523  480 iKQNLEQKQkelKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
                          330
                   ....*....|...
gi 528501420   651 EEagkiVQDSLNQ 663
Cdd:TIGR04523  560 EK----EIDEKNK 568
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
326-666 2.82e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 61.39  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   326 VVETEDLVDTDI-PPLTGTGDSKFDDLFGTSAATDPFNFNSQNGMRkddkdrliEQLTAELQALKEELESFRLESGRLCQ 404
Cdd:pfam12128  554 VISPELLHRTDLdPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE--------EELRERLDKAEEALQSAREKQAAAEE 625
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   405 ALRGRVNELEAELAEQThLKQQALGESEflraelDDLRRVKEDTEKEQRSLSE--IERKAQANEQRyTKLKEKYTELVQS 482
Cdd:pfam12128  626 QLVQANGELEKASREET-FARTALKNAR------LDLRRLFDEKQSEKDKKNKalAERKDSANERL-NSLEAQLKQLDKK 697
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   483 HADLLRKNAEVTRQMTVAR-AAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSR-----------TEL 550
Cdd:pfam12128  698 HQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkREI 777
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   551 ETLKSTVTSSQQsNEQLGTQL-----SALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNER---ESGVKAAEALQN 622
Cdd:pfam12128  778 RTLERKIERIAV-RRQEVLRYfdwyqETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRaklEMERKASEKQQV 856
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528501420   623 QLNEKESREQALESELVSLRwasLRAALEEAGKIVQDSLNQLED 666
Cdd:pfam12128  857 RLSENLRGLRCEMSKLATLK---EDANSEQAQGSIGERLAQLED 897
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
376-665 2.87e-09

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: 61.24  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   376 RLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQthlkQQALG--ESEFLRAELDDLRRVKEDTEKEQR 453
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHKL----EEALNdlEARLSHSRIPEIQAELSKLEEEVS 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   454 SLSEIERKAQANEQRYTKLKEKYTELVQshaDLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQdsasqqekAQL 533
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQ---ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE--------AAL 877
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   534 EQLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNEresg 613
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLREL---ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE---- 950
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501420   614 vKAAEALQNQLNEKESREQALES---------ELVSLRWASL---RAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02169  951 -LSLEDVQAELQRVEEEIRALEPvnmlaiqeyEEVLKRLDELkekRAKLEEERKAILERIEEYE 1013
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
378-576 4.23e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRlesgrlcqALRGRVNELEAELAEQthlkQQALGEsefLRAELDDLRRVKEDTEKEQRsLSE 457
Cdd:COG4717    73 LKELEEELKEAEEKEEEYA--------ELQEELEELEEELEEL----EAELEE---LREELEKLEKLLQLLPLYQE-LEA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  458 IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 528501420  538 ALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVA 576
Cdd:COG4717   217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
370-602 6.94e-09

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: 60.07  E-value: 6.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR----VK 445
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanLR 823
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   446 EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSA 525
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   526 SQQEKAQLE---QLQALQAELMSSRTELETLKSTVTSSQQS-NEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELER 601
Cdd:TIGR02168  904 RELESKRSElrrELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983

                   .
gi 528501420   602 L 602
Cdd:TIGR02168  984 L 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
436-665 1.56e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  436 AELDDLRRvkedtEKEQRsLSEIERKA-QAneQRYTKLKEKYTELvQSHADLLRKNaEVTRQMTVARAAQDEVENVKKEM 514
Cdd:COG1196   189 ERLEDILG-----ELERQ-LEPLERQAeKA--ERYRELKEELKEL-EAELLLLKLR-ELEAELEELEAELEELEAELEEL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  515 QDRLKVAQ------DSASQQEKAQLEQLQALQAELMSSRTELET----LKSTVTSSQQSNEQLGTQLSALVAEKAGLVET 584
Cdd:COG1196   259 EAELAELEaeleelRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  585 VSRKEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLrwASLRAALEEAGKIVQDSLNQL 664
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERL 416

                  .
gi 528501420  665 E 665
Cdd:COG1196   417 E 417
PTZ00121 PTZ00121
MAEBL; Provisional
418-666 2.49e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  418 AEQTHLKQQALGESEFLRAELDDLRRvKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSH----ADLLRKNAEV 493
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkkADELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  494 TRQMTVARAAQDEVENVKKEMQDRlkvAQDSASQQEKAQLEQLQALQAELMSSRTEL------ETLKSTVTSSQQSNEQL 567
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeAKIKAEELKKAEEEKKK 1634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  568 GTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSS-------LTNERESGVKAAEALQNQLNEKESREQALESELVS 640
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
                         250       260
                  ....*....|....*....|....*.
gi 528501420  641 LRWASLRAALEEAGKIVQDSLNQLED 666
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAE 1740
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
370-613 2.61e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRL-------------IEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHLKQQALGESEF--L 434
Cdd:COG4913   591 EKDDRRRIrsryvlgfdnrakLAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasA 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  435 RAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEM 514
Cdd:COG4913   667 EREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  515 Q------DRLKVAQDSASQQEKAQLE-QLQALQAELMSSRTELETL-----------KSTVTSSQQSNEQLGTQLSALVA 576
Cdd:COG4913   747 LralleeRFAAALGDAVERELRENLEeRIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPEYLALLDRLEE 826
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 528501420  577 EkaGLVETVSR-KEVELSGLGAELERLQSSLTNERESG 613
Cdd:COG4913   827 D--GLPEYEERfKELLNENSIEFVADLLSKLRRAIREI 862
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
372-636 3.28e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  372 DDKDRLIEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHLKQqalgesefLRAELDDLRRVKEDTEKe 451
Cdd:PRK03918  448 EHRKELLEEYTAELKRIEKELK----EIEEKERKLRKELRELEKVLKKESELIK--------LKELAEQLKELEEKLKK- 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  452 qRSLSEIERKAQaneqRYTKLKEKYTEL---VQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLK--------- 519
Cdd:PRK03918  515 -YNLEELEKKAE----EYEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvee 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  520 ---------------VAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSalVAEKAGLVET 584
Cdd:PRK03918  590 leerlkelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREE 667
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528501420  585 VSRKEVELSGLGAELERLQSSltneRESGVKAAEALQNQLNEKESREQALES 636
Cdd:PRK03918  668 YLELSRELAGLRAELEELEKR----REEIKKTLEKLKEELEEREKAKKELEK 715
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
389-665 3.43e-08

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: 57.83  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   389 KEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQA--LGESEFLRAELD-DLRRVKEdtEKEQRSLSEIERKAQAN 465
Cdd:pfam17380  295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiYAEQERMAMERErELERIRQ--EERKRELERIRQEEIAM 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   466 EQrytklkEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAElms 545
Cdd:pfam17380  373 EI------SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE--- 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   546 SRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGL-VETVSRKEVELSG---LGAELE-RLQSSLTNERESGV--KAAE 618
Cdd:pfam17380  444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRrkiLEKELEeRKQAMIEEERKRKLleKEME 523
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 528501420   619 ALQNQLNEKESREQAlESELVSLRWASLRAALEEAGKIVQDSLNQLE 665
Cdd:pfam17380  524 ERQKAIYEEERRREA-EEERRKQQEMEERRRIQEQMRKATEERSRLE 569
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
371-652 3.80e-08

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 57.21  E-value: 3.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   371 KDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGrVNELEAELAEQTHLKQQALGESEFLRAELDDlrRVKEDTEK 450
Cdd:pfam07888   68 REQWERQRRELESRVAELKEELRQSREKHEELEEKYKE-LSASSEELSEEKDALLAQRAAHEARIRELEE--DIKTLTQR 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   451 EQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTR---QMTVARAAQDE-------VENVKKEMQDRLKV 520
Cdd:pfam07888  145 VLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSlskEFQELRNSLAQrdtqvlqLQDTITTLTQKLTT 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   521 AQDSASQQEkAQLEQLQALQAELMSSRTELETLKSTVTS--SQQSN------------EQLGTQLSAL-----------V 575
Cdd:pfam07888  225 AHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSmaAQRDRtqaelhqarlqaAQLTLQLADAslalregrarwA 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   576 AEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGVKAAEALQnqlNEKE-SREQALES--ELVSLRwASLRAALEE 652
Cdd:pfam07888  304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG---REKDcNRVQLSESrrELQELK-ASLRVAQKE 379
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
412-665 7.56e-08

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: 56.61  E-value: 7.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   412 ELEAELAEQTHLKQQALGESEFLRAELDDLR-RVKEDTEK---EQRSLSEIERKAQANEQRYTKLKEKYTELvqshadll 487
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDELSQElsdASRKIGEIEKEIEQLEQEEEKLKERLEEL-------- 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   488 rknaevtrqMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQlEQLQALQAELMSSR-----TELETLKSTVTSSQQ 562
Cdd:TIGR02169  743 ---------EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE-EALNDLEARLSHSRipeiqAELSKLEEEVSRIEA 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   563 SNEQLGTQLSALVAEKAGLVETVSRKEVELsglgAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLR 642
Cdd:TIGR02169  813 RLREIEQKLNRLTLEKEYLEKEIQELQEQR----IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
                          250       260
                   ....*....|....*....|...
gi 528501420   643 waSLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02169  889 --KERDELEAQLRELERKIEELE 909
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
367-666 1.01e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  367 NGMRKDDKDRLIEQLTAELQAL---KEELESFRLESGRLCQALRGRVNELEAELAEqthLKQqALGESEFLRAELDD--- 440
Cdd:PRK03918  375 ERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEE---LKK-AKGKCPVCGRELTEehr 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  441 ---LRRVK---EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSH--ADLLRKNAEVTRQMTV--ARAAQDEVENV 510
Cdd:PRK03918  451 kelLEEYTaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKLKKYNLeeLEKKAEEYEKL 530
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  511 KKEMqDRLKVAQDSAsqqeKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEV 590
Cdd:PRK03918  531 KEKL-IKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  591 ELSGLGAELERLQSSLTNERESGVKA----------AEALQNQLNEKESR-----EQALESELVSLR--WASLRAALEEA 653
Cdd:PRK03918  606 ELKDAEKELEREEKELKKLEEELDKAfeelaetekrLEELRKELEELEKKyseeeYEELREEYLELSreLAGLRAELEEL 685
                         330
                  ....*....|...
gi 528501420  654 GKIVQDSLNQLED 666
Cdd:PRK03918  686 EKRREEIKKTLEK 698
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
372-652 1.47e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.89  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   372 DDKDRLIEQLTAELQALKEELESfrlESGRLCQALRGRVNELEaelaEQTHLKQQALGESEFLRAELDDLRRVKEDTEKE 451
Cdd:pfam15921  422 DDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLE----KVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   452 QR-------SLSEIERKAQANEQRYTKLKE----KYTEL------------VQSHADLLR-------KNAEVTRQ----M 497
Cdd:pfam15921  495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhlknegdhlrnVQTECEALKlqmaekdKVIEILRQqienM 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   498 T--------VARAAQDEVENVKKEMQDR---------LKVAQDSASQQEKAQLEQLQALQAELMSS-----------RTE 549
Cdd:pfam15921  575 TqlvgqhgrTAGAMQVEKAQLEKEINDRrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAgserlravkdiKQE 654
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   550 LETLKSTVTSSQQSNEQLGTQLSAL---VAEKAGLVETVSRK-EVELSGLGAELERLQSSLTNERES---GVKAAEALQN 622
Cdd:pfam15921  655 RDQLLNEVKTSRNELNSLSEDYEVLkrnFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSdghAMKVAMGMQK 734
                          330       340       350
                   ....*....|....*....|....*....|
gi 528501420   623 QLNEKESREQALESELVSLRWASLRAALEE 652
Cdd:pfam15921  735 QITAKRGQIDALQSKIQFLEEAMTNANKEK 764
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
378-584 2.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESGRLCQAL-RGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR------------V 444
Cdd:COG4913   264 YAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdrleqL 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  445 KEDTEKEQRSLSEIERKAQANEQRYTKLKEkytELVQSHADLLRKNAEVTRQMTVARAAQDEVENvkkemqdrlkvAQDS 524
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALGL---PLPASAEEFAALRAEAAALLEALEEELEALEE-----------ALAE 409
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  525 ASQQEKAQLEQLQALQAELmssrTELETLKSTVTSSQQsneqlgtQLSALVAEKAGLVET 584
Cdd:COG4913   410 AEAALRDLRRELRELEAEI----ASLERRKSNIPARLL-------ALRDALAEALGLDEA 458
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
42-126 2.91e-07

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 50.35  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   42 VSINKAINTQEVAVKEKHARTCILGTH-HEKGAHTFWL--AVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:cd03564     3 VAVVKATNHDEVPPKEKHVRKLLLATSnGGGRADVAYIvhALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82

                  ....*...
gi 528501420  119 ADLNDMSR 126
Cdd:cd03564    83 GHIFNLSN 90
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
364-638 3.05e-07

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: 54.64  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   364 NSQNGMRKDDKdrLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlKQQALGESEFLRAELDDLRR 443
Cdd:TIGR04523  325 EIQNQISQNNK--IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE----NQSYKQEIKNLESQINDLES 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   444 VKEDTEKEQRslsEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQD 523
Cdd:TIGR04523  399 KIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   524 SAsQQEKAQLEQLQAlqaELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ 603
Cdd:TIGR04523  476 SI-NKIKQNLEQKQK---ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528501420   604 SSLT-------------------NERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:TIGR04523  552 FELKkenlekeideknkeieelkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
426-737 6.04e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  426 QALGESEFLRAELDDLRRVKEDTEKEqrsLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMtvaRAAQD 505
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  506 EVENVKKEMQ----------------------DRLkVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQS 563
Cdd:COG3883    87 ELGERARALYrsggsvsyldvllgsesfsdflDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  564 NEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRW 643
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  644 ASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALDCVERLRSSRDGFVSDNTDVSGLVRAVTQFAHLVGD 723
Cdd:COG3883   246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGG 325
                         330
                  ....*....|....
gi 528501420  724 VIVQGSATSHMVPV 737
Cdd:COG3883   326 ASAGGGGGSGGGGG 339
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
384-652 6.59e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 6.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  384 ELQALKEELESFRLESGRLcqalRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQ 463
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  464 ANEQRYTKLKEKYTELVQSHADL---LRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDsaSQQEKAQLEQ-LQAL 539
Cdd:PRK03918  249 SLEGSKRKLEEKIRELEERIEELkkeIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEeINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  540 QAELmssrTELETLKSTVTSSQQSNEQLGTQLSALvAEKAGLVETVSRKEVELSGLGAELERLQ-SSLTNERESGVKAAE 618
Cdd:PRK03918  327 EERI----KELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKE 401
                         250       260       270
                  ....*....|....*....|....*....|....
gi 528501420  619 ALQNQLNEKESREQALESELvslrwASLRAALEE 652
Cdd:PRK03918  402 EIEEEISKITARIGELKKEI-----KELKKAIEE 430
PRK11281 PRK11281
mechanosensitive channel MscK;
411-663 7.06e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 53.76  E-value: 7.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  411 NELEAeLAEQTHLK------QQALGESEFLraeLDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKytelvqsha 484
Cdd:PRK11281   43 AQLDA-LNKQKLLEaedklvQQDLEQTLAL---LDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD--------- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  485 dllrkNAEVTRQmTVARAAQdevenvkKEMQDRLKVAQDsasQQEKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSN 564
Cdd:PRK11281  110 -----NDEETRE-TLSTLSL-------RQLESRLAQTLD---QLQNAQ-NDLAEYNSQLVSLQTQPERAQAALYANSQRL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  565 EQLGTQLSALVAEKAGLVET-VSRKEVELSGLGAELERLQSSLTNEresgVKAAEALQNQLNEKESREQALESELVSLRW 643
Cdd:PRK11281  173 QQIRNLLKGGKVGGKALRPSqRVLLQAEQALLNAQNDLQRKSLEGN----TQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
                         250       260
                  ....*....|....*....|
gi 528501420  644 ASLRAALEEAGKIVQDSLNQ 663
Cdd:PRK11281  249 AINSKRLTLSEKTVQEAQSQ 268
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
370-642 1.53e-06

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: 52.42  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   370 RKDDKDRLIEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHL---KQQALGESEFLRAELDDLRRVKE 446
Cdd:pfam05483  371 RLEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQELIFLLQ 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   447 DTEKEQRSLSEIERKAQANEQRYTK-LKEKYTEL---------VQSHAD-LLRKNAEVTRQmtvaraAQDEVENVKKEMQ 515
Cdd:pfam05483  447 AREKEIHDLEIQLTAIKTSEEHYLKeVEDLKTELekeklknieLTAHCDkLLLENKELTQE------ASDMTLELKKHQE 520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   516 DrlkvaQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGL 595
Cdd:pfam05483  521 D-----IINCKKQEERMLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420   596 GAELERLQSSLTN----------ERESGVKAAEALQNQLNEKESREQALESELVSLR 642
Cdd:pfam05483  593 ENKCNNLKKQIENknknieelhqENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
410-633 1.89e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  410 VNEL-EAELAEQTHLKQQALGES-EFLRAELDDLRRVKEDTE------KEQRSLSEIERKAQANEQRYTKLKEKYTEL-- 479
Cdd:COG3206   154 ANALaEAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEAra 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  480 ----VQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDrLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKS 555
Cdd:COG3206   234 elaeAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  556 TVTSSQQSN-EQLGTQLSALVAEKAGL---VETVSRKEVELSGLGAELERLQSSLtneresgvkaaEALQNQLNEKESRE 631
Cdd:COG3206   313 RILASLEAElEALQAREASLQAQLAQLearLAELPELEAELRRLEREVEVARELY-----------ESLLQRLEEARLAE 381

                  ..
gi 528501420  632 QA 633
Cdd:COG3206   382 AL 383
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
436-650 2.70e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  436 AELDDLRRVKEDTEKEQRSLSEIERKAQ--------ANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEV 507
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELAEryaaarerLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  508 ENVKKEMQDRLKVAQDsasQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSR 587
Cdd:COG4913   315 EARLDALREELDELEA---QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501420  588 KEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRwASLRAAL 650
Cdd:COG4913   392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR-DALAEAL 453
PTZ00121 PTZ00121
MAEBL; Provisional
370-655 2.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAeqthlKQQALGESEFLRaELDDLRRVKEDTE 449
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKKAEEKKK 1291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKA-----QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDS 524
Cdd:PTZ00121 1292 ADEAKKAEEKKKAdeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  525 ASQQEKAQLEQL-----QALQAELMSSRTE-----LETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSG 594
Cdd:PTZ00121 1372 KKEEAKKKADAAkkkaeEKKKADEAKKKAEedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501420  595 lGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGK 655
Cdd:PTZ00121 1452 -KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
369-525 3.18e-06

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 51.24  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  369 MRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQAlrgRVNELEAELAEqthlkqqalgesefLRAELDDLrrvKEDT 448
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFE---RLAELRDELAE--------------LEEELEAL---KARW 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKN------------AEVTRQMT---VARAAQDEVENVKKe 513
Cdd:COG0542   464 EAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELApllreevteediAEVVSRWTgipVGKLLEGEREKLLN- 542
                         170
                  ....*....|....*
gi 528501420  514 MQDRLK---VAQDSA 525
Cdd:COG0542   543 LEEELHervIGQDEA 557
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-638 3.73e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  369 MRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRG---RVNELEA---ELAEQTHLKQQALGESEFLRAELDDLR 442
Cdd:PRK03918  186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKlekEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELE 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  443 RVKEDTEKEQRSLSEIER---KAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVK-------- 511
Cdd:PRK03918  266 ERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerleelkk 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  512 --KEMQDRLKVAQDSASQQE--KAQLEQLQALQAELmsSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSR 587
Cdd:PRK03918  346 klKELEKRLEELEERHELYEeaKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528501420  588 KEVELSGL----------GAEL-----ERLQSSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:PRK03918  424 LKKAIEELkkakgkcpvcGRELteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
384-601 3.96e-06

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 50.14  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   384 ELQALKEELESFRLESGRLCQALRGRVNELeaelaeQTHLKQQALGESEFLRAELDDLRRvkedtEKEQrSLSEIERKAQ 463
Cdd:pfam09787    1 NLESAKQELADYKQKAARILQSKEKLIASL------KEGSGVEGLDSSTALTLELEELRQ-----ERDL-LREEIQKLRG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   464 ANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAEL 543
Cdd:pfam09787   69 QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEI 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420   544 MSSRTELeTLKSTVTSSQQSNE-----------QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELER 601
Cdd:pfam09787  149 EKLRNQL-TSKSQSSSSQSELEnrlhqltetliQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSN 216
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
375-630 4.12e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  375 DRLIEQLTaELQALKEELESFRLESGRLcQALRGRVNELEAELAEQTHLKQqalgesefLRAELDDLRRvkedtekeQRS 454
Cdd:COG4913   228 DALVEHFD-DLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEY--------LRAALRLWFA--------QRR 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMtvARAAQDEVENVKKEMqDRLKVAQDSASQQEKAQLE 534
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREI-ERLERELEERERRRARLEA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  535 QLQALQAELMSSRTELETLKSTVTSSQqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGV 614
Cdd:COG4913   367 LLAALGLPLPASAEEFAALRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
                         250
                  ....*....|....*.
gi 528501420  615 KAAEALQNQLNEKESR 630
Cdd:COG4913   444 ALRDALAEALGLDEAE 459
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
369-634 4.47e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.89  E-value: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   369 MRKDDKDRLIEQLT---AELQALKEELESFRLESG-------RLCQALRGRVNELEAELAEQTHLKQQALGES---EFLR 435
Cdd:pfam15921  339 MYEDKIEELEKQLVlanSELTEARTERDQFSQESGnlddqlqKLLADLHKREKELSLEKEQNKRLWDRDTGNSitiDHLR 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   436 AELDDLRRVKEDTEKEQRSLS-----EIERKAQANEQRYTKLkEKYTEL---VQSHADLLRKNAE--VTRQMTVaRAAQD 505
Cdd:pfam15921  419 RELDDRNMEVQRLEALLKAMKsecqgQMERQMAAIQGKNESL-EKVSSLtaqLESTKEMLRKVVEelTAKKMTL-ESSER 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   506 EVENVKKEMQDRLKVAQDSASQQEKA------QLEQLQALQAE---LMSSRTELETLKSTVTSSQQSNEQLGTQLS---- 572
Cdd:pfam15921  497 TVSDLTASLQEKERAIEATNAEITKLrsrvdlKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtq 576
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   573 ----------ALVAEKAGLVETVSRKEVELSGLGA----------ELERLQSSLTNERESGVKA-AEALQNQLNEKESRE 631
Cdd:pfam15921  577 lvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKIlkdkkdakirELEARVSDLELEKVKLVNAgSERLRAVKDIKQERD 656

                   ...
gi 528501420   632 QAL 634
Cdd:pfam15921  657 QLL 659
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
378-586 5.09e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESGRLcqALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRvkedtekeQRSLSE 457
Cdd:COG3206   184 LPELRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA--------QLGSGP 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  458 IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:COG3206   254 DALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQ 333
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528501420  538 ALQAELMS-------SRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVS 586
Cdd:COG3206   334 AQLAQLEArlaelpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
370-551 6.56e-06

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: 49.76  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFR---LESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRV-- 444
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQLAALErriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAly 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  445 -------------KEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVK 511
Cdd:COG4942   115 rlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 528501420  512 KEMQDRLKVAQDSASQQEkAQLEQLQALQAELMSSRTELE 551
Cdd:COG4942   195 AERQKLLARLEKELAELA-AELAELQQEAEELEALIARLE 233
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
371-635 6.60e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  371 KDDKDRLIEQLTAELQAlKEELEsfrlesgrlcqaLRGRVNELEAELAEQTHL-------KQQA----------LGESEF 433
Cdd:PRK02224  182 LSDQRGSLDQLKAQIEE-KEEKD------------LHERLNGLESELAELDEEieryeeqREQAretrdeadevLEEHEE 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  434 LRAELDDLrrvKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKE 513
Cdd:PRK02224  249 RREELETL---EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  514 MQDRL---KVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEV 590
Cdd:PRK02224  326 LRDRLeecRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 528501420  591 ELSGLGAELERLQSSLTNERESgVKAAEA-LQNQLNEKESREQALE 635
Cdd:PRK02224  406 DLGNAEDFLEELREERDELRER-EAELEAtLRTARERVEEAEALLE 450
PTZ00121 PTZ00121
MAEBL; Provisional
370-666 8.53e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 8.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  530 KAQLEQLQalQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERlqssltnE 609
Cdd:PTZ00121 1545 KKKADELK--KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------A 1615
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420  610 RESGVKaAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLED 666
Cdd:PTZ00121 1616 EEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
PTZ00121 PTZ00121
MAEBL; Provisional
386-537 9.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  386 QALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEK---EQRSLSEIERKA 462
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKA 1690
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501420  463 QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVEnvKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK--KEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
mukB PRK04863
chromosome partition protein MukB;
376-661 1.12e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  376 RLIEQLTAELQALKEELESFRLESGRLCQALR---------GRVNELEAELAEQTHLKQQAlgeseflRAELDDLRRVKE 446
Cdd:PRK04863  314 RELAELNEAESDLEQDYQAASDHLNLVQTALRqqekieryqADLEELEERLEEQNEVVEEA-------DEQQEENEARAE 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  447 DTEKE-----------QRSLSEIERKAQANEQRYTKLkEKYTELVQShADLLRKNAEVTrqMTVARAAQDEVENVKKEMQ 515
Cdd:PRK04863  387 AAEEEvdelksqladyQQALDVQQTRAIQYQQAVQAL-ERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLE 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  516 DRLKVAQDSASQQEKA-------------------------QLEQLQALQAELMSSRTELETLKSTVtSSQQSNEQLGTQ 570
Cdd:PRK04863  463 QKLSVAQAAHSQFEQAyqlvrkiagevsrseawdvarellrRLREQRHLAEQLQQLRMRLSELEQRL-RQQQRAERLLAE 541
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  571 LSalvaEKAGLVETvsrKEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESElvSLRWASLRAAL 650
Cdd:PRK04863  542 FC----KRLGKNLD---DEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR--APAWLAAQDAL 612
                         330
                  ....*....|.
gi 528501420  651 EEAGKIVQDSL 661
Cdd:PRK04863  613 ARLREQSGEEF 623
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
368-666 1.17e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.44  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   368 GMRKDDKDRLieqltaelQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQ-------------------QAL 428
Cdd:pfam10174   46 ALRKEEAARI--------SVLKEQYRVTQEEN----QHLQLTIQALQDELRAQRDLNQllqqdfttspvdgedkfstPEL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   429 GESEFLRAELDDLRRVKEdTEKEQRSLSEIERKAQANEQRYTKLKE---KYTELVQSHADLLRKNAEV---TRQMTVARA 502
Cdd:pfam10174  114 TEENFRRLQSEHERQAKE-LFLLRKTLEEMELRIETQKQTLGARDEsikKLLEMLQSKGLPKKSGEEDwerTRRIAEAEM 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   503 A---------QDEVENV--KKEMQDRLKVAQDSASQQEKAQL-----EQLQALQAELMSSRTELETLKST-VTSSQQSNE 565
Cdd:pfam10174  193 QlghlevlldQKEKENIhlREELHRRNQLQPDPAKTKALQTViemkdTKISSLERNIRDLEDEVQMLKTNgLLHTEDREE 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   566 QLgTQL------SALVAEKAG-LVETVSRKEVELSGLGAELErlqsSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:pfam10174  273 EI-KQMevykshSKFMKNKIDqLKQELSKKESELLALQTKLE----TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
                          330       340
                   ....*....|....*....|....*...
gi 528501420   639 VSLRwasLRaaLEEAGKIVQDSLNQLED 666
Cdd:pfam10174  348 DALR---LR--LEEKESFLNKKTKQLQD 370
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
493-665 1.23e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  493 VTRQMTVARAAQDEVENVKKEMQDRLKVAQD------------SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSS 560
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  561 QQSNE----------------QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNEREsgvKAAEALQNQL 624
Cdd:COG3206   246 RAQLGsgpdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ---RILASLEAEL 322
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528501420  625 NEKESREQALESELvslrwASLRAALEEAGKIVQDsLNQLE 665
Cdd:COG3206   323 EALQAREASLQAQL-----AQLEARLAELPELEAE-LRRLE 357
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
369-517 2.01e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  369 MRKDDKDRLIEQLTAELQAL--------KEELESfRLESGRLCQALRGRVNELEAELAEQTHLKQQAL--GESEFLRAEL 438
Cdd:COG4717   356 AEELEEELQLEELEQEIAALlaeagvedEEELRA-ALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEEL 434
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420  439 DDLRRVKEDTEKEQRSLSEiERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDR 517
Cdd:COG4717   435 EELEEELEELEEELEELRE-ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
371-636 2.02e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.63  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   371 KDDKDRLIEQLTAELQAL----------KEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELD- 439
Cdd:pfam01576  652 KEELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFEr 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   440 DLRRVKEDTEKEQRSLS----------EIERKAQANEQRYTKLKEKYTELVQSHADLLRKNA-EVTRQMtvaRAAQDEVE 508
Cdd:pfam01576  732 DLQARDEQGEEKRRQLVkqvreleaelEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGReEAVKQL---KKLQAQMK 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   509 NVKKEMQDrLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRK 588
Cdd:pfam01576  809 DLQRELEE-ARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRL 887
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528501420   589 EVELSGLGAELERLQSS--LTNER-ESGVKAAEALQNQLNEKESREQALES 636
Cdd:pfam01576  888 EARIAQLEEELEEEQSNteLLNDRlRKSTLQVEQLTTELAAERSTSQKSES 938
PTZ00121 PTZ00121
MAEBL; Provisional
371-655 2.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  371 KDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNEleAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEK 450
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  451 --EQRSLSEIERKAQANEQRYTKLKEKYTElvQSHADLLRK-----NAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQD 523
Cdd:PTZ00121 1479 aeEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKaeeakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  524 SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGlGAELERLQ 603
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKV 1635
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528501420  604 SSLTNERESGVKAAEALQNQLNEKESR--EQALESELVSLRWASLRAALEEAGK 655
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKK 1689
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
525-666 2.70e-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: 46.84  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  525 ASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQS 604
Cdd:COG1579     1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528501420  605 SLTNEResGVKAAEALQNQLNEKESREQALESELVSL--RWASLRAALEEAGKIVQDSLNQLED 666
Cdd:COG1579    81 QLGNVR--NNKEYEALQKEIESLKRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEE 142
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
438-660 2.83e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  438 LDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTEL--VQSHADLLRKNAEVTRQ-MTVARAAQDEvenvkkem 514
Cdd:PRK10929   57 LEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVppNMSTDALEQEILQVSSQlLEKSRQAQQE-------- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  515 QDRLKVAQDSASQQEKAQLEQLQALQAelMSSRteLETLKSTVTSSQQSneqlgtQLSALVAEKAGLVETVSrkEVELSG 594
Cdd:PRK10929  129 QDRAREISDSLSQLPQQQTEARRQLNE--IERR--LQTLGTPNTPLAQA------QLTALQAESAALKALVD--ELELAQ 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  595 LGA----ELERLQSSLTNEResgvkaAEALQNQLnekesreQALESELVSLRWASLRAALEEAGKIVQDS 660
Cdd:PRK10929  197 LSAnnrqELARLRSELAKKR------SQQLDAYL-------QALRNQLNSQRQREAERALESTELLAEQS 253
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
372-694 2.95e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.41  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  372 DDKDRLIE------QLTAELQALKEELESFRLESGRLCQALRGR---------VNELEAELAEQTHL-----KQQALGES 431
Cdd:COG3096   303 EEQYRLVEmareleELSARESDLEQDYQAASDHLNLVQTALRQQekieryqedLEELTERLEEQEEVveeaaEQLAEAEA 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  432 EFLRAElDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLkEKYTELVQShADLLRKNAEvTRQMTvARAAQDEVENVK 511
Cdd:COG3096   383 RLEAAE-EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL-EKARALCGL-PDLTPENAE-DYLAA-FRAKEQQATEEV 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  512 KEMQDRLKVAQDSASQQEKA--------------------------------QLEQLQALQAELMSSRTELETLKSTVTS 559
Cdd:COG3096   458 LELEQKLSVADAARRQFEKAyelvckiageversqawqtarellrryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERL 537
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  560 SQQSNEQLGTQLSALvaekaglvetvsrkevelsglgAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELV 639
Cdd:COG3096   538 LEEFCQRIGQQLDAA----------------------EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 528501420  640 SLRwaslraALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQValdcVERLR 694
Cdd:COG3096   596 ELA------ARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL----LERER 640
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
500-653 3.49e-05

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 47.15  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  500 ARAAQDEVENVKKEMQD---RLKVAQD------------SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSN 564
Cdd:COG3524   172 ERAREDAVRFAEEEVERaeeRLRDAREallafrnrngilDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQV 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  565 EQLGTQLSAL----VAEKAGLVETVSRKevELSGLGAELERLQssltneresgvkaaealqnqlNEKESREQALESELvs 640
Cdd:COG3524   252 RQLRRRIAALekqiAAERARLTGASGGD--SLASLLAEYERLE---------------------LEREFAEKAYTSAL-- 306
                         170
                  ....*....|...
gi 528501420  641 lrwASLRAALEEA 653
Cdd:COG3524   307 ---AALEQARIEA 316
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
366-635 5.36e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   366 QNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEA---EL------------------AEQTHLK 424
Cdd:pfam01576  254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlktELedtldttaaqqelrskreQEVTELK 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   425 QQALGESEFLRAELDDLRR--------VKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQ 496
Cdd:pfam01576  334 KALEEETRSHEAQLQEMRQkhtqaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   497 MTVARAAQDEVENVKKEMQDRLKVAQ---DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSA 573
Cdd:pfam01576  414 LQELQARLSESERQRAELAEKLSKLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528501420   574 LVAEKAGLVETVSRKEVELSGLGAELERLQSSLTN-----ERESGV------------KAAEALQNQLNEKESREQALE 635
Cdd:pfam01576  494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDmkkklEEDAGTlealeegkkrlqRELEALTQQLEEKAAAYDKLE 572
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
428-611 6.05e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  428 LGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTEL--VQSHADLLRKNAEVTRQMtvaRAAQD 505
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAEL---AELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  506 EVENVKKEMQDRlkvaqdsasqqeKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSN-EQLGTQLSALVAEKAGLVET 584
Cdd:COG4717   147 RLEELEERLEEL------------RELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEE 214
                         170       180
                  ....*....|....*....|....*..
gi 528501420  585 VSRKEVELSGLGAELERLQSSLTNERE 611
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAAL 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
374-626 6.37e-05

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: 46.94  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   374 KDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDL----RRVKEDTE 449
Cdd:TIGR04523  361 KQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLekeiERLKETII 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLR--KNAEVTRQMTVARAAQDEVE-----NVKKEMQDRLKVAQ 522
Cdd:TIGR04523  437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKELKSKEKElkklnEEKKELEEKVKDLT 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   523 DSASQ---------QEKAQLEQ-----------------LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVA 576
Cdd:TIGR04523  517 KKISSlkekiekleSEKKEKESkisdledelnkddfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   577 EKAGLVETVSRKEVELSGLGAELERLQ----------SSLTNERESGVKAAEALQNQLNE 626
Cdd:TIGR04523  597 EKKDLIKEIEEKEKKISSLEKELEKAKkeneklssiiKNIKSKKNKLKQEVKQIKETIKE 656
mukB PRK04863
chromosome partition protein MukB;
374-713 6.47e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.26  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  374 KDRLIEQLTAELQALKEELESFRLESgRLCQ---------------------------ALRGRVNELEAELAEQ------ 420
Cdd:PRK04863  784 REKRIEQLRAEREELAERYATLSFDV-QKLQrlhqafsrfigshlavafeadpeaelrQLNRRRVELERALADHesqeqq 862
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  421 -----THLKQQALG------------------ESEFLRAELDDLRRVKEDTEKEQRSLSEIERKA---QANEQRYTKLKE 474
Cdd:PRK04863  863 qrsqlEQAKEGLSAlnrllprlnlladetladRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVsvlQSDPEQFEQLKQ 942
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  475 KYTELVQSHADLLRKNAEVT--RQMTVARAAQDEVENVKK--EMQDRLKVAQDSASQQEKAQLEQLQALQAE-------L 543
Cdd:PRK04863  943 DYQQAQQTQRDAKQQAFALTevVQRRAHFSYEDAAEMLAKnsDLNEKLRQRLEQAEQERTRAREQLRQAQAQlaqynqvL 1022
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  544 MSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKA---------GLVETVSRKEvelsglgaELERLQSSLTNERESGV 614
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERArarrdelhaRLSANRSRRN--------QLEKQLTFCEAEMDNLT 1094
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  615 KAAEALQNQLneKESREQALESElvsLRWASLRAALEEAGkiVQDSLNQlEDPAHIsctsSADYLVSRCQVALdcvERLR 694
Cdd:PRK04863 1095 KKLRKLERDY--HEMREQVVNAK---AGWCAVLRLVKDNG--VERRLHR-RELAYL----SADELRSMSDKAL---GALR 1159
                         410
                  ....*....|....*....
gi 528501420  695 SSrdgfVSDNTDVSGLVRA 713
Cdd:PRK04863 1160 LA----VADNEHLRDVLRL 1174
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
373-578 9.10e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   373 DKDRLIEQL----TAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQ-----------THLKQQALGESEFLRAE 437
Cdd:pfam10174  447 EKERIIERLkeqrEREDRERLEELESLKKEN----KDLKEKVSALQPELTEKesslidlkehaSSLASSGLKKDSKLKSL 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   438 LDDLRRVKEDTEKEQRSL---SEIERKAQANEQRYTKLKEKYTElVQSHADLLRK-NAEVTRQMTVARAAQDE------- 506
Cdd:pfam10174  523 EIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQE-VARYKEESGKaQAEVERLLGILREVENEkndkdkk 601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   507 ------------------VENVK-KEMQDRLKVAQ-------DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSS 560
Cdd:pfam10174  602 iaelesltlrqmkeqnkkVANIKhGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST 681
                          250
                   ....*....|....*...
gi 528501420   561 QQSNEQLGTQLSALVAEK 578
Cdd:pfam10174  682 QQSLAEKDGHLTNLRAER 699
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
437-664 1.66e-04

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: 44.21  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   437 ELDDLRRVKEDTEKEQRSLSEIER------KAQANEQRytklKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENV 510
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQalslldKIDASKQR----AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   511 K---KEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVET-VS 586
Cdd:pfam12795   77 SlslEELEQRLLQTSAQLQELQ----NQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAqRW 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   587 RKEVELSGLGAE---LERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQ 663
Cdd:pfam12795  153 ALQAELAALKAQidmLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232

                   .
gi 528501420   664 L 664
Cdd:pfam12795  233 H 233
PRK12704 PRK12704
phosphodiesterase; Provisional
371-515 1.93e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  371 KDDKDRLIEQLTAELQALKEELEsfrLESGRLCQALRgrvNELEAELAEQT-HLKQQalgESEFLRAElDDLRRVKEDTE 449
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLR---NEFEKELRERRnELQKL---EKRLLQKE-ENLDRKLELLE 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528501420  450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLrknaEVTRQMTVARAAQDEVENVKKEMQ 515
Cdd:PRK12704  107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAEEAKEILLEKVEEEAR 168
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
435-642 2.04e-04

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: 45.44  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   435 RAELDDLRRVKEDTEKEQRSLSEIE-----------------------RKAQANEQRYTKLKEK-----YTELVQSHADL 486
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEeveenierldliidekrqqlerlRREREKAERYQALLKEkreyeGYELLKEKEAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   487 LRKNAEVTRQMTVARAAQD----EVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   563 SNEQLGTQLSALVAEkaglvetVSRKEVELSGLGAELERLQ---SSLTNERESGVKAAEALQNQLNEKESREQALESELV 639
Cdd:TIGR02169  316 ELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388

                   ...
gi 528501420   640 SLR 642
Cdd:TIGR02169  389 DYR 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
370-551 2.05e-04

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: 45.44  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlKQQALGEsefLRAELDDLRRVKEDTE 449
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE----LEAALRD---LESRLGDLKKERDELE 895
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   450 KE----QRSLSEIERKAQANEQRYTKLKEKYTELVQSHA---DLLRKNAEVTRQMTVARAAQDEVENVKKEMQD----RL 518
Cdd:TIGR02169  896 AQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNM 975
                          170       180       190
                   ....*....|....*....|....*....|...
gi 528501420   519 KVAQDSASqqEKAQLEQLQALQAELMSSRTELE 551
Cdd:TIGR02169  976 LAIQEYEE--VLKRLDELKEKRAKLEEERKAIL 1006
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
476-643 2.26e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 43.00  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   476 YTELVQSHADLLRKnaevtrqmtvARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTEL-ETLK 554
Cdd:pfam08614    2 FLELIDAYNRLLDR----------TALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELaELYR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   555 STVTSSQQ---SNEQLGT----------QLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLtneresgvkaaEALQ 621
Cdd:pfam08614   72 SRGELAQRlvdLNEELQElekklrederRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDEL-----------VALQ 140
                          170       180
                   ....*....|....*....|....*
gi 528501420   622 NQLNEKESREQALESE---LVSlRW 643
Cdd:pfam08614  141 LQLNMAEEKLRKLEKEnreLVE-RW 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
484-642 2.39e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  484 ADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQ----------DSASQQE-----KAQLEQLQALQAELMSSRT 548
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeiDVASAEReiaelEAELERLDASSDDLAALEE 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  549 ELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQSSLTNER-------ESGVKAAEALQ 621
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaalgdAVERELRENLE 772
                         170       180
                  ....*....|....*....|.
gi 528501420  622 NQLNEKESREQALESELVSLR 642
Cdd:COG4913   773 ERIDALRARLNRAEEELERAM 793
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
369-635 3.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  369 MRKDDKDRLIEQLTAELQALKEELEsfRLESGRLCQALRGRVNELEAELAEQT-HLKQQALGESEFLRaeLDDLRRVKED 447
Cdd:COG1196   513 ALLLAGLRGLAGAVAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAAAAIeYLKAAKAGRATFLP--LDKIRARAAL 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  448 TEKEQRSLSEIERKAQANEQRYTKLKEK---YTELVQSHADLLRKNA------------EVTRQMTVARAAQDEVENVKK 512
Cdd:COG1196   589 AAALARGAIGAAVDLVASDLREADARYYvlgDTLLGRTLVAARLEAAlrravtlagrlrEVTLEGEGGSAGGSLTGGSRR 668
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  513 EMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKstvtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVEL 592
Cdd:COG1196   669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA------EAEEERLEEELEEEALEEQLEAEREELLEELL 742
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 528501420  593 SGLGAELERLQSSLTNEREsgvkaAEALQNQLNEKESREQALE 635
Cdd:COG1196   743 EEEELLEEEALEELPEPPD-----LEELERELERLEREIEALG 780
PRK11637 PRK11637
AmiB activator; Provisional
377-543 3.20e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  377 LIEQLTAELQALKEELESFRLESGRLcQALRGRVNELEAELAeqtHLKQQALGESEFLRAELDDLRRV-----------K 445
Cdd:PRK11637   73 LLAQLKKQEEAISQASRKLRETQNTL-NQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  446 EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLkVAQDSA 525
Cdd:PRK11637  149 EESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTL-TGLESS 227
                         170
                  ....*....|....*...
gi 528501420  526 SQQEKAQLEQLQALQAEL 543
Cdd:PRK11637  228 LQKDQQQLSELRANESRL 245
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
383-567 3.75e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 43.09  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   383 AELQALKEELESFRlesgrlcqalrGRVNELEAELAEQTHLKQQALGESEFLRAEL----DDLRRVKEDTEKEQRSLSE- 457
Cdd:pfam00261    1 KKMQQIKEELDEAE-----------ERLKEAMKKLEEAEKRAEKAEAEVAALNRRIqlleEELERTEERLAEALEKLEEa 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   458 -------------IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTV-------ARAAQDEVENVKKEMQDR 517
Cdd:pfam00261   70 ekaadesergrkvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVvegdlerAEERAELAESKIVELEEE 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   518 LKVA----------QDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQL 567
Cdd:pfam00261  150 LKVVgnnlksleasEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
361-670 3.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  361 FNFNSQNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDD 440
Cdd:COG4372    16 FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  441 LRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQmtvARAAQDEVENVKKEMQDRLKV 520
Cdd:COG4372    96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE---LKELEEQLESLQEELAALEQE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  521 AQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELE 600
Cdd:COG4372   173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  601 RLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHI 670
Cdd:COG4372   253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
402-666 4.85e-04

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: 44.33  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   402 LCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEierkaqaNEQRYTKLKEKYTELVQ 481
Cdd:pfam05483  262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-------DLQIATKTICQLTEEKE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   482 SHADLLRKnAEVTRQMTVAraaqdEVENVKKEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELETLKSTVTSSQ 561
Cdd:pfam05483  335 AQMEELNK-AKAAHSFVVT-----EFEATTCSLEELLRTEQQRLEKNE----DQLKIITMELQKKSSELEEMTKFKNNKE 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   562 QSNEQLGTQLS---ALVAEKA---GLVETVSRKEVELSGLGA-------ELERLQSSLTNERESGVKAAEALQNQL-NEK 627
Cdd:pfam05483  405 VELEELKKILAedeKLLDEKKqfeKIAEELKGKEQELIFLLQarekeihDLEIQLTAIKTSEEHYLKEVEDLKTELeKEK 484
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 528501420   628 -ESREQALESELVSLRWASLraaLEEAGKIVQDSLNQLED 666
Cdd:pfam05483  485 lKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQED 521
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
379-641 5.22e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   379 EQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAElddlRRVKEDTEKEQRSLSEI 458
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK----REAQEEQLKKQQLLKQL 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   459 ERK---AQANEQRYTKLKEKYTE-------------LVQSHADLLRKNAEVTRQMTvaraaqdeveNVKKEMQDRLKVAQ 522
Cdd:TIGR00618  266 RARieeLRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMR----------SRAKLLMKRAAHVK 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   523 DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERL 602
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 528501420   603 QSSLTNERESGVKAAEALQNQLNEKESREQALESELVSL 641
Cdd:TIGR00618  416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
Filament pfam00038
Intermediate filament protein;
373-653 5.53e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   373 DKDRLIEQLTAELQA-LKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRrVKEDTEKE 451
Cdd:pfam00038   18 DKVRFLEQQNKLLETkISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR-QKYEDELN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   452 QRSLSEIE---RKAQANEQRYTKLK-EKYTELVQSHADLLRKN--AEVtRQMTvaraAQDEVENVKKEMQDRLKVAQDSA 525
Cdd:pfam00038   97 LRTSAENDlvgLRKDLDEATLARVDlEAKIESLKEELAFLKKNheEEV-RELQ----AQVSDTQVNVEMDAARKLDLTSA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   526 SQQEKAQLEQLQALqaelmsSRTELEtlkstvtssqqsnEQLGTQLSALVAEKAGLVETVSRKEVELSglgaELERLQSS 605
Cdd:pfam00038  172 LAEIRAQYEEIAAK------NREEAE-------------EWYQSKLEELQQAAARNGDALRSAKEEIT----ELRRTIQS 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 528501420   606 LTNERESGVKAAEALQNQLNEKESReqaLESELVSLRwaSLRAALEEA 653
Cdd:pfam00038  229 LEIELQSLKKQKASLERQLAETEER---YELQLADYQ--ELISELEAE 271
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
432-666 5.56e-04

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: 44.01  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   432 EFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKytelVQSHADLLRKnAEVTRQMTVARaaQDEVENVK 511
Cdd:pfam01576    5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQ----LQAETELCAE-AEEMRARLAAR--KQELEEIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   512 KEMQDRLKVAQDSASQ--QEKAQLEQ-LQALQAEL---MSSRTELETLKSTVTSSQQSNEQ----LGTQLSALVAEKAGL 581
Cdd:pfam01576   78 HELESRLEEEEERSQQlqNEKKKMQQhIQDLEEQLdeeEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSKLSKERKLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   582 VETVSrkevELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALE----------SEL------VSLRWAS 645
Cdd:pfam01576  158 EERIS----EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkakrklegesTDLqeqiaeLQAQIAE 233
                          250       260
                   ....*....|....*....|.
gi 528501420   646 LRAALEEAGKIVQDSLNQLED 666
Cdd:pfam01576  234 LRAQLAKKEEELQAALARLEE 254
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
362-601 5.64e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   362 NFNSQNGMRKDDKDRLIEQLTAELQAlKEELESFRLESGRLCQALRGRVNELEAEL--AEQTHLKQQaLGESEFLRAELD 439
Cdd:TIGR00606  394 NFHTLVIERQEDEAKTAAQLCADLQS-KERLKQEQADEIRDEKKGLGRTIELKKEIleKKQEELKFV-IKELQQLEGSSD 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   440 DLRRVKEDTEKEQRSLSEIERKA--QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvaraAQDEVENVKKEMQDR 517
Cdd:TIGR00606  472 RILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT----TRTQMEMLTKDKMDK 547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   518 LKVAQDSASQQE------------KAQLEQ-LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVET 584
Cdd:TIGR00606  548 DEQIRKIKSRHSdeltsllgyfpnKKQLEDwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
                          250       260
                   ....*....|....*....|...
gi 528501420   585 V------SRKEVELSGLGAELER 601
Cdd:TIGR00606  628 LfdvcgsQDEESDLERLKEEIEK 650
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
333-638 6.69e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 6.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   333 VDTDIPPLTGTgdskfddLFGTSAATDPFNFNSQNGMR------KDDKDRLIEQLTAELQALKEELESFRLESGR----- 401
Cdd:pfam15921  229 LDTEISYLKGR-------IFPVEDQLEALKSESQNKIElllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSiqsql 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   402 --------------LCQ--ALRGRVNELEAELAEQTHL---------KQQALGESEFLRAE------------LDD-LRR 443
Cdd:pfam15921  302 eiiqeqarnqnsmyMRQlsDLESTVSQLRSELREAKRMyedkieeleKQLVLANSELTEARterdqfsqesgnLDDqLQK 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   444 VKEDTEKEQRSLSeIERkaQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENvkkEMQDRLKVAQD 523
Cdd:pfam15921  382 LLADLHKREKELS-LEK--EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   524 SASQQEK-----AQLEQ----LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSG 594
Cdd:pfam15921  456 KNESLEKvssltAQLEStkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH 535
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 528501420   595 LGAELERLQSSLTNeresgvkaAEALQNQLNEKESREQALESEL 638
Cdd:pfam15921  536 LKNEGDHLRNVQTE--------CEALKLQMAEKDKVIEILRQQI 571
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
456-653 6.70e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   456 SEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQ 535
Cdd:pfam12128  269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   536 LQALQAELMSSRTELETLkstvTSSQQSNEQLGTQLSALVAEKaglvetvsrkevelsgLGAELERLQSSLTNERESGVK 615
Cdd:pfam12128  349 LPSWQSELENLEERLKAL----TGKHQDVTAKYNRRRSKIKEQ----------------NNRDIAGIKDKLAKIREARDR 408
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 528501420   616 AAEALQNQLnekesreQALESELVSLRWASLRAALEEA 653
Cdd:pfam12128  409 QLAVAEDDL-------QALESELREQLEAGKLEFNEEE 439
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
378-652 7.33e-04

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 43.48  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   378 IEQLTAELQALKEELESFRL-----ESGRLCQALRGRvnelEAELAEQTHLKQqalgeseflrAElDDLRRVKEDTekeq 452
Cdd:pfam05701  182 VEELTIELIATKESLESAHAahleaEEHRIGAALARE----QDKLNWEKELKQ----------AE-EELQRLNQQL---- 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   453 RSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvaRAAQDEVENVKKEMQD-RLKVaqdsasqqEKA 531
Cdd:pfam05701  243 LSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTS--TSIQAALASAKKELEEvKANI--------EKA 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   532 QLEqLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAE---KAGLVETVSRKEVELSGLGAELERLQSSLTN 608
Cdd:pfam05701  313 KDE-VNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAElnrTKSEIALVQAKEKEAREKMVELPKQLQQAAQ 391
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 528501420   609 ERESGVKAAEALQNQLNE-KESREQALESelVSLRWASLRAALEE 652
Cdd:pfam05701  392 EAEEAKSLAQAAREELRKaKEEAEQAKAA--ASTVESRLEAVLKE 434
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
424-655 9.40e-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: 43.19  E-value: 9.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   424 KQQalgESEFLRAELDDLRRVKEDTEKE---QRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVA 500
Cdd:pfam17380  287 RQQ---QEKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   501 RAAQDEVENVKKEMQ--DRLKVAQDSASQQEKAQLE---QLQALQAELMSSRTELETLKSTVTSSQQSNEQLgtQLSALV 575
Cdd:pfam17380  364 RIRQEEIAMEISRMRelERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLE 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   576 AEKAGLVETVSRKEVELSglgAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRwaslRAALEEAGK 655
Cdd:pfam17380  442 EERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK----QAMIEEERK 514
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
352-666 9.72e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.02  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  352 FGTSAATDPFNFNSQNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQaLRGRVNELEAELAEQTHLKQQALGES 431
Cdd:COG5185   195 LKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELED-LAQTSDKLEKLVEQNTDLRLEKLGEN 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  432 EflraelDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEkytelvqshadlLRKNAEVTRQMtvarAAQDEVENVK 511
Cdd:COG5185   274 A------ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA------------TESLEEQLAAA----EAEQELEESK 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  512 KEMQDRLKVAQDSASQQEKAQLEQLQALQAELMS---------SRTELETLKSTVTSSQQSNEQLGTQLSALVAE-KAGL 581
Cdd:COG5185   332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIENivgevelskSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLATL 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  582 VETVSRKEVELsglgAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSL 661
Cdd:COG5185   412 EDTLKAADRQI----EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEEL 487

                  ....*
gi 528501420  662 NQLED 666
Cdd:COG5185   488 TQIES 492
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
404-648 9.87e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  404 QALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRV---------------KEDTEKEQRSLSEIERKAQANEQR 468
Cdd:COG3096   839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLlpqanlladetladrLEELREELDAAQEAQAFIQQHGKA 918
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  469 YTKLKEKYTEL---VQSHADLLRKNAEVTRQMTVARAA----------------QDEVENVKK--EMQDRLKVAQDSASQ 527
Cdd:COG3096   919 LAQLEPLVAVLqsdPEQFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyEDAVGLLGEnsDLNEKLRARLEQAEE 998
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  528 QEKAQLEQLQALQAELMSSRTELETLKS-------TVTSSQQSNEQLGTQLSALVAEKAGlvETVSRKEVELSGLGAELE 600
Cdd:COG3096   999 ARREAREQLRQAQAQYSQYNQVLASLKSsrdakqqTLQELEQELEELGVQADAEAEERAR--IRRDELHEELSQNRSRRS 1076
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501420  601 RLQSSLT-NERESgvkaaEALQNQLNEKESREQALESELVS--LRWASLRA 648
Cdd:COG3096  1077 QLEKQLTrCEAEM-----DSLQKRLRKAERDYKQEREQVVQakAGWCAVLR 1122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
471-641 1.06e-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: 41.83  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  471 KLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQD-RLKVAQ-DSASQQEKAQLEQLQALQAELMSSRt 548
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlEKEIKRlELEIEEVEARIKKYEEQLGNVRNNK- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  549 ELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQssltNERESGVKAAEALQNQLNEK- 627
Cdd:COG1579    90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK----AELDEELAELEAELEELEAEr 165
                         170
                  ....*....|....
gi 528501420  628 ESREQALESELVSL 641
Cdd:COG1579   166 EELAAKIPPELLAL 179
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
436-638 1.11e-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: 41.83  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  436 AELDDLRRVKEDTEKEqrsLSEIERKAQANEQRYTKLKEKYTELvqsHADLLRKNAEVtrqmtvaraaqDEVENVKKEMQ 515
Cdd:COG1579    17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDL---EKEIKRLELEI-----------EEVEARIKKYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  516 DRLKVAQDSasqqekaqlEQLQALQAELmssrteletlkstvtssqqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGL 595
Cdd:COG1579    80 EQLGNVRNN---------KEYEALQKEI---------------------ESLKRRISDLEDEILELMERIEELEEELAEL 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 528501420  596 GAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:COG1579   130 EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
377-665 1.17e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   377 LIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQrsls 456
Cdd:TIGR00618  401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---- 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   457 eierKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQdrlkvaqdsASQQEKAQLEQ- 535
Cdd:TIGR00618  477 ----TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ---------RGEQTYAQLETs 543
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   536 LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGL----------VETVSRKEVELSGLG-AELERLQS 604
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitvrlqdlTEKLSEAEDMLACEQhALLRKLQP 623
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501420   605 SLTNERESGV--KAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR00618  624 EQDLQDVRLHlqQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
370-653 1.23e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLEsgrlCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:PRK02224  357 RAEELREEAAELESELEEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  450 KEQRSLSEIERKAQA-------------------------NEQRYTKLKEKYTELVQSHADLlrkNAEVTRQMTVARAAQ 504
Cdd:PRK02224  433 ATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEV---EERLERAEDLVEAED 509
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  505 --DEVENVKKEMQDRLKVAQDSA-SQQEKAQL--EQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKA 579
Cdd:PRK02224  510 riERLEERREDLEELIAERRETIeEKRERAEElrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501420  580 GLvETVSRKEVELSGLGAELERLqssltNERESGVKAAEAL-QNQLNEKESREQALESELVSLRWASLRAALEEA 653
Cdd:PRK02224  590 SL-ERIRTLLAAIADAEDEIERL-----REKREALAELNDErRERLAEKRERKRELEAEFDEARIEEAREDKERA 658
PRK09039 PRK09039
peptidoglycan -binding protein;
370-443 1.80e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528501420  370 RKDDKDRLIEQLTAEL---QALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR 443
Cdd:PRK09039   75 GNQDLQDSVANLRASLsaaEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRR 151
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
379-665 1.85e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   379 EQLTAELQALKEELESFRLESGR-----------LCQALRGRVNELEAELAEQTHLKQQALGESEFLraeLDDLRRVKED 447
Cdd:pfam12128  386 EQNNRDIAGIKDKLAKIREARDRqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLR---LNQATATPEL 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   448 TEKEQRSLSEIERKAQANEQRytklkekytelvqshadllRKNAE-VTRQMTVARAAQDEvenvkkemqdrlkvaQDSAS 526
Cdd:pfam12128  463 LLQLENFDERIERAREEQEAA-------------------NAEVErLQSELRQARKRRDQ---------------ASEAL 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   527 QQEKAQLEQLQALQAELM-----SSRTELETLKSTVTSSQQS------NEQLGTqlSALVAEkagLVETVSRKEVELSGL 595
Cdd:pfam12128  509 RQASRRLEERQSALDELElqlfpQAGTLLHFLRKEAPDWEQSigkvisPELLHR--TDLDPE---VWDGSVGGELNLYGV 583
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501420   596 GAELERLQ--SSLTNE---RESGVKAAEALQNQlnekESREQALESELVslrwaSLRAALEEAGKIVQDSLNQLE 665
Cdd:pfam12128  584 KLDLKRIDvpEWAASEeelRERLDKAEEALQSA----REKQAAAEEQLV-----QANGELEKASREETFARTALK 649
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
502-658 2.28e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  502 AAQDEVENVKKEMQDRLKVAQDSASQ-QEKAQ--LEQLQALQAELMSSRTELETLKSTVtssqqsNEQLGTQLSALVAEk 578
Cdd:cd22656   107 TDDEELEEAKKTIKALLDDLLKEAKKyQDKAAkvVDKLTDFENQTEKDQTALETLEKAL------KDLLTDEGGAIARK- 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  579 aglvetvsrkevELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWA--SLRAALEEAGKI 656
Cdd:cd22656   180 ------------EIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDldNLLALIGPAIPA 247

                  ..
gi 528501420  657 VQ 658
Cdd:cd22656   248 LE 249
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
434-555 2.75e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   434 LRAELDDLRRVKEDTEKEQRSLSEiERKAQAneQRYTKLKEKYTELVQSHadllrknAEVTRQMTVARAAQDEVENVKKE 513
Cdd:pfam07926    6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLH-------AEDIKALQALREELNELKAEIAE 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 528501420   514 MQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKS 555
Cdd:pfam07926   76 LKAEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNE 117
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
432-566 2.93e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.53  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   432 EFLRAELD-DLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELvQSHADLLRKNAEVTRQMTvaRAAQDEVENV 510
Cdd:pfam05262  184 EALREDNEkGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKA-QQKADFAQDNADKQRDEV--RQKQQEAKNL 260
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501420   511 KK-----EMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQ 566
Cdd:pfam05262  261 PKpadtsSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAED 321
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
378-658 3.62e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  378 IEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSE 457
Cdd:COG1340     3 TDELSSSLEELEEKIEELREEI----EELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  458 --IERKAQANE--QRYTKLKEKYTELVQSHADL--LRK--NAEVTRQMTVARAAQDEVENVKK--EMQDRLKVAQDSASQ 527
Cdd:COG1340    79 erDELNEKLNElrEELDELRKELAELNKAGGSIdkLRKeiERLEWRQQTEVLSPEEEKELVEKikELEKELEKAKKALEK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  528 QEKaqleqLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEkaglVETVsRKEVElsGLGAELERLQsslt 607
Cdd:COG1340   159 NEK-----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE----ADEL-RKEAD--ELHKEIVEAQ---- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528501420  608 neresgvKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQ 658
Cdd:COG1340   223 -------EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
379-573 3.69e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  379 EQLTAELQALKEEL---ESFRLESGRLCQALRGRVNELEAELAEQT-------HLKQQAL-GESEFLRAELDDLRRVKED 447
Cdd:COG3096   451 QQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTarellrrYRSQQALaQRLQQLRAQLAELEQRLRQ 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  448 TEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKV---AQDS 524
Cdd:COG3096   531 QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDA 610
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 528501420  525 ASQ---QEKAQLEQLQALQA---ELMSSRTELETLKSTVTSSQQSNEQLGTQLSA 573
Cdd:COG3096   611 LERlreQSGEALADSQEVTAamqQLLEREREATVERDELAARKQALESQIERLSQ 665
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
381-669 4.28e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   381 LTAELQALKEELESFRLESgrlcqalrGRVNELEAELaeQTHLKQQalgeseflrAELDDLRR-VKedtEKEQRSLSEIE 459
Cdd:pfam05622  109 LAEEAQALKDEMDILRESS--------DKVKKLEATV--ETYKKKL---------EDLGDLRRqVK---LLEERNAEYMQ 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   460 RKAQANEQrytklkekytelvqshadlLRKnaevtrqmtvARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLE----- 534
Cdd:pfam05622  167 RTLQLEEE-------------------LKK----------ANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkle 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   535 -QLQALQAELMSSRTELETLKSTVTS---SQQSNEQLgTQLSALVAEKAGLVETVSrKEVELSGLGAELERLQSS----L 606
Cdd:pfam05622  218 eKLEALQKEKERLIIERDTLRETNEElrcAQLQQAEL-SQADALLSPSSDPGDNLA-AEIMPAEIREKLIRLQHEnkmlR 295
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501420   607 TNERESGVKAAEALQNQLNEKESREQALESE--LVSLRWASLRAALEEAGKIVQDSLNQLEDPAH 669
Cdd:pfam05622  296 LGQEGSYRERLTELQQLLEDANRRKNELETQnrLANQRILELQQQVEELQKALQEQGSKAEDSSL 360
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
372-580 4.31e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  372 DDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTH-LKQQA---------------LGESEFLR 435
Cdd:COG3883    40 DALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERREeLGERAralyrsggsvsyldvLLGSESFS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  436 AELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQ 515
Cdd:COG3883   116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528501420  516 DRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAG 580
Cdd:COG3883   196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
PTZ00121 PTZ00121
MAEBL; Provisional
391-637 4.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  391 ELESFRLESGRLCQALRGRVNELEAELAEQTHLK--QQALGESEFLRAEldDLRRVKEDTEKEQRSLSEIERKAQ----- 463
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaEDARKAEEARKAE--DARKAEEARKAEDAKRVEIARKAEdarka 1166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  464 -----ANEQRYTKLKEKYTELvqSHADLLRKnAEVTRQMTVARAAQDE--VENVKK-------EMQDRLKVAQDSASQQE 529
Cdd:PTZ00121 1167 eearkAEDAKKAEAARKAEEV--RKAEELRK-AEDARKAEAARKAEEErkAEEARKaedakkaEAVKKAEEAKKDAEEAK 1243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  530 KAQLEQLQALQAELMSSRTELETLKSTVTSSQQSN--EQLGTQLSALVAEKAGLVETVsrKEVELSGLGAELERLQSSLT 607
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADEAK 1321
                         250       260       270
                  ....*....|....*....|....*....|
gi 528501420  608 NERESGVKAAEALQNQLNEKESREQALESE 637
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
526-640 4.95e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.13  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   526 SQQEKAQL-EQLQALQAELMSSRTELETLKST----VTSSQQSNEQLGTQLSAlvaekaglvETVSRKEVElsglgAELE 600
Cdd:pfam09787   52 LRQERDLLrEEIQKLRGQIQQLRTELQELEAQqqeeAESSREQLQELEEQLAT---------ERSARREAE-----AELE 117
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528501420   601 RLQSSLTNERESGVKAAEALQNQLNEKESREQALESELVS 640
Cdd:pfam09787  118 RLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTS 157
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
375-586 5.19e-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: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  375 DRLIEQLTAELQALKEELEsfrlesgrlcqalrgrvnELEAELAEqthlkqqalgesefLRAELDDLRRVKEDTEKEQRs 454
Cdd:COG1579    16 DSELDRLEHRLKELPAELA------------------ELEDELAA--------------LEARLEAAKTELEDLEKEIK- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  455 lsEIERKAQANEQRYTKLKEKYTElvqshadlLRKNAEVTrqmtvarAAQDEVENVKKEMQDRLKVAQDSASQQEKAQlE 534
Cdd:COG1579    63 --RLELEIEEVEARIKKYEEQLGN--------VRNNKEYE-------ALQKEIESLKRRISDLEDEILELMERIEELE-E 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528501420  535 QLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVS 586
Cdd:COG1579   125 ELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKIP 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-497 5.70e-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: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196   684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528501420  450 KEQRSLSEIERKAQA----N----------EQRYTKLKEKYTELVQSHADLLRKNAEVTRQM 497
Cdd:COG1196   764 ELERELERLEREIEAlgpvNllaieeyeelEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
366-638 5.73e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   366 QNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGR------VNELEAELAEQTHLKQQALGEsefLRAELD 439
Cdd:TIGR00606  360 QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQedeaktAAQLCADLQSKERLKQEQADE---IRDEKK 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   440 DLRRV----KEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADL--LRKNAEVTRQMTVARAAQDEVENVKKE 513
Cdd:TIGR00606  437 GLGRTielkKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskAEKNSLTETLKKEVKSLQNEKADLDRK 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   514 MQdrlKVAQDSAS-QQEKAQLEQLQALQAELMSSRTELETLKstvtsSQQSNEQLGtqLSALVAEKAGLVETVSRKEVEL 592
Cdd:TIGR00606  517 LR---KLDQEMEQlNHHTTTRTQMEMLTKDKMDKDEQIRKIK-----SRHSDELTS--LLGYFPNKKQLEDWLHSKSKEI 586
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 528501420   593 SGLGAELERLQSSLtneresgvKAAEALQNQLNEKESREQALESEL 638
Cdd:TIGR00606  587 NQTRDRLAKLNKEL--------ASLEQNKNHINNELESKEEQLSSY 624
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
525-621 6.75e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  525 ASQQEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ 603
Cdd:COG4942    17 AQADAAAEAEaELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                          90
                  ....*....|....*...
gi 528501420  604 SSLTNERESGVKAAEALQ 621
Cdd:COG4942    97 AELEAQKEELAELLRALY 114
PRK01156 PRK01156
chromosome segregation protein; Provisional
370-663 7.00e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEE-LESFRLESGRLcqALRGRVNELEAELAEQTHLKQQalgesefLRAELDDLRRVKEDT 448
Cdd:PRK01156  136 GQGEMDSLISGDPAQRKKILDEiLEINSLERNYD--KLKDVIDMLRAEISNIDYLEEK-------LKSSNLELENIKKQI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTR-QMTVARA----AQDEVENVK-KEMQDRLKVAQ 522
Cdd:PRK01156  207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyESEIKTAesdlSMELEKNNYyKELEERHMKII 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  523 DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVtssqQSNEQLGTQLSALVAEKAGLVETVSRKEvELSGLGAELERL 602
Cdd:PRK01156  287 NDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEI----NKYHAIIKKLSVLQKDYNDYIKKKSRYD-DLNNQILELEGY 361
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528501420  603 QS----------SLTNERESGVKAAEALQNQLNEKESREQALESELVSlRWASLRAALEE-AGKIvqDSLNQ 663
Cdd:PRK01156  362 EMdynsylksieSLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK-ELNEINVKLQDiSSKV--SSLNQ 430
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
379-637 7.04e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.55  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  379 EQLTAELQALKEELESFRLESGRLCQALR--GRVNELEAELAEQTHLKQQALGESEFLRAELDDL------RRVKEDTEK 450
Cdd:PRK10246  219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALslaqpaRQLRPHWER 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  451 EQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEvtRQMTVARAAQDEVENvkkemqDRLKV-AQDSAS--- 526
Cdd:PRK10246  299 IQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAE--LQAQQQSLNTWLAEH------DRFRQwNNELAGwra 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  527 --QQEKAQLEQLQALQAELMSSRTELETL-KSTVTSS--------QQSNEQ--LGTQLSALVAEKAGLVETVSRKEVELS 593
Cdd:PRK10246  371 qfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTadevaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQ 450
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 528501420  594 GLGAELERLQSSLTNERESGVKAAEALQN--QLNEKESREQALESE 637
Cdd:PRK10246  451 NVTQEQTQRNAALNEMRQRYKEKTQQLADvkTICEQEARIKDLEAQ 496
PRK12705 PRK12705
hypothetical protein; Provisional
413-543 7.38e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  413 LEAELAEQTHLKQQALGES--EFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKN 490
Cdd:PRK12705   39 LQEAQKEAEEKLEAALLEAkeLLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528501420  491 AevtrqmtvaraaqdEVENVKKEMQDRLKVAQDSASQQEKAQLeqLQALQAEL 543
Cdd:PRK12705  119 L--------------ELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAEL 155
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-553 7.60e-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: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLR-RVKEDT 448
Cdd:COG1196   631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeEERELA 710
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQD----RLKVAQDS 524
Cdd:COG1196   711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvNLLAIEEY 790
                         170       180
                  ....*....|....*....|....*....
gi 528501420  525 ASQQEkaQLEQLQALQAELMSSRTELETL 553
Cdd:COG1196   791 EELEE--RYDFLSEQREDLEEARETLEEA 817
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
497-637 8.06e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153338 [Multi-domain]  Cd Length: 264  Bit Score: 39.49  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  497 MTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQqsneqlgtQLSALVA 576
Cdd:cd07654    80 DAVAQSRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQAEVQQTVRELSKSRKTYFERE--------QVAHLAR 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501420  577 EKAGLVEtvsrkevelsglgAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESE 637
Cdd:cd07654   152 EKAADVQ-------------AREARSDLSIFQSRTSLQKASVKLSARKAECSSKATAARND 199
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
379-637 8.43e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   379 EQLTAELQALKEELESFRLESGRL---CQALRGRVNELEAELAEQTHLKQQ-ALGES-----EFLRAEL--DDLRRVKED 447
Cdd:pfam05622  207 DKLEFEYKKLEEKLEALQKEKERLiieRDTLRETNEELRCAQLQQAELSQAdALLSPssdpgDNLAAEImpAEIREKLIR 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   448 TEKEQRSLSEieRKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAqdeVENVKKEMQDRLKVAQDSASQ 527
Cdd:pfam05622  287 LQHENKMLRL--GQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ---VEELQKALQEQGSKAEDSSLL 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420   528 QEK--AQLEQLQALQAELMSSRTELETLKSTVTSS-QQSNEQLGTQLSALVAEKAGLVETVSR-----KEVeLSGLGAel 599
Cdd:pfam05622  362 KQKleEHLEKLHEAQSELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEDMKAMEERYKKyvekaKSV-IKTLDP-- 438
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 528501420   600 eRLQSSLTNEresgvkaAEALQNQLNEKESREQALESE 637
Cdd:pfam05622  439 -KQNPASPPE-------IQALKNQLLEKDKKIEHLERD 468
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
505-661 8.43e-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: 39.14  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  505 DEVENVKKEMQDRLKVAQDsasqqEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQQ----SNEQLGT-----QLSAL 574
Cdd:COG1579    20 DRLEHRLKELPAELAELED-----ELAALEaRLEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLGNvrnnkEYEAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501420  575 VAEKAGLVETVSRKEVELSGLGAELERLQSSLTNERESGVKAAEALQNQLNEKESREQALESELvslrwASLRAALEEAG 654
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-----EELEAEREELA 169

                  ....*..
gi 528501420  655 KIVQDSL 661
Cdd:COG1579   170 AKIPPEL 176
 
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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