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Conserved domains on  [gi|2462613984|ref|XP_054214016|]
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huntingtin-interacting protein 1 isoform X3 [Homo sapiens]

Protein Classification

ANTH domain-containing protein( domain architecture ID 13730376)

ANTH (AP180 N-Terminal Homology) domain-containing protein similar to Caenorhabditis elegans huntington interacting protein related 1 (HIP1) 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
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
785-983 3.70e-95

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


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 299.28  E-value: 3.70e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   785 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 864
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   865 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 943
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462613984   944 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 983
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
12-277 6.01e-94

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: 299.21  E-value: 6.01e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   12 TVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:pfam07651    3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   91 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 169
Cdd:pfam07651   83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  170 FQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 243
Cdd:pfam07651  161 QKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  244 FYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 277
Cdd:pfam07651  240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
453-551 1.56e-34

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: 127.05  E-value: 1.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 2462613984  533 SEANWAAEFAELEKERDSL 551
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
341-615 5.61e-18

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: 89.61  E-value: 5.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 419
Cdd:COG1196    219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 499
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462613984  580 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196    455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
 
Name Accession Description Interval E-value
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
785-983 3.70e-95

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 299.28  E-value: 3.70e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   785 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 864
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   865 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 943
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462613984   944 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 983
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
12-277 6.01e-94

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: 299.21  E-value: 6.01e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   12 TVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:pfam07651    3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   91 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 169
Cdd:pfam07651   83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  170 FQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 243
Cdd:pfam07651  161 QKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  244 FYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 277
Cdd:pfam07651  240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
11-124 2.76e-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: 2.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   11 ETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:cd17013      1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462613984   91 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
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 ...
835-981 6.51e-60

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: 201.27  E-value: 6.51e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  835 KNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVN 914
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  915 QATAGVVASTISGKSQIEE--TDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYE 981
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
9-131 8.04e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 8.04e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984     9 PPETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVLKDSL 86
Cdd:smart00273    1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEAL 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462613984    87 RYRNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTKMEYHTKNPRFP 131
Cdd:smart00273   81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
453-551 1.56e-34

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: 127.05  E-value: 1.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 2462613984  533 SEANWAAEFAELEKERDSL 551
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
341-615 5.61e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.61  E-value: 5.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 419
Cdd:COG1196    219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 499
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462613984  580 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196    455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
348-615 1.84e-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: 75.09  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAeqqhlrqqaADDCEFLRAELDELRRQREDTE----KA 421
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALL---------VLRLEELREELEELQEELKEAEeeleEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLErisdQGQRKTQE 501
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----ELESKLDE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  582 SMCQLAKDQRKMLlvgsRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168  415 RRERLQQEIEELL----KKLEEAELKELQAELEE 444
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
406-591 1.13e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.48  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  406 AELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaEVTKQVSMARQAQVDLEREKKELE 485
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELP 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  486 DSLERIsdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLETS-AQSEANWAAEFAELEKERDSLVSGAAHREEELSA 564
Cdd:COG4717    146 ERLEEL--------EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
                          170       180
                   ....*....|....*....|....*..
gi 2462613984  565 LRKELQDTQLKLASTEESMCQLAKDQR 591
Cdd:COG4717    218 AQEELEELEEELEQLENELEAAALEER 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
342-778 1.71e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMK------TESQRVVLQLKGHVSELEADLAEQQHLRQQaaddcefLRAELDELRRQR 415
Cdd:PRK03918   210 NEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKV 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  416 EDTEKAQ------RSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLE 489
Cdd:PRK03918   283 KELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  490 RISDQGQRKTQeqlevLESLKQELATS-----QRELQVLQGSLETSAQSEANWAAEFAELEKERDSL------------- 551
Cdd:PRK03918   363 LYEEAKAKKEE-----LERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgk 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  552 --VSGAA----HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkaaEQVIqdalnqLEEPPLISCAGSA 625
Cdd:PRK03918   438 cpVCGRElteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------EKVL------KKESELIKLKELA 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  626 DHLLSTVTSISSC-IEQLEKSWSQYLACPE-------DISGLLHSITLLAHLTSDAIAhgattCLRAPPEPADSLTEACK 697
Cdd:PRK03918   503 EQLKELEEKLKKYnLEELEKKAEEYEKLKEkliklkgEIKSLKKELEKLEELKKKLAE-----LEKKLDELEEELAELLK 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  698 QYGRETLAYLASLEEE-GSLENADSTAMRncLSKIKAIGEELLPRgLDIKQEELgDLVDKEMAATSAAIETATARIEEML 776
Cdd:PRK03918   578 ELEELGFESVEELEERlKELEPFYNEYLE--LKDAEKELEREEKE-LKKLEEEL-DKAFEELAETEKRLEELRKELEELE 653

                   ..
gi 2462613984  777 SK 778
Cdd:PRK03918   654 KK 655
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
354-615 5.00e-09

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: 60.57  E-value: 5.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  354 EISGLKAQLE---NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIER 430
Cdd:pfam01576  244 ELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  431 KaqaNEQRYSKLKEKYSELVQNH----ADLLRKNA----EVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQ 502
Cdd:pfam01576  324 K---REQEVTELKKALEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL--------QAE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  503 LEVLESLKQELATSQR----ELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:pfam01576  393 LRTLQQAKQDSEHKRKklegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462613984  579 TEEsmcQLAKDQRKMLLVGSRKAAEQVIQDAL-NQLEE 615
Cdd:pfam01576  473 TQE---LLQEETRQKLNLSTRLRQLEDERNSLqEQLEE 507
mukB PRK04863
chromosome partition protein MukB;
382-565 3.51e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 58.04  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  382 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:PRK04863   500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQVSMARQAQVDLEREKKELE----------DSLERISDQ-GQrkTQEQLEVLESLKQELATSQRELQVLQGSLETS 530
Cdd:PRK04863   576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsGE--EFEDSQDVTEYMQQLLERERELTVERDELAAR 653
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462613984  531 AQSeanwaaefaeLEKERDSLVSGAAHREEELSAL 565
Cdd:PRK04863   654 KQA----------LDEEIERLSQPGGSEDPRLNAL 678
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
404-588 3.07e-07

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: 54.69  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  404 LRAELDELRRQREDTEKAQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK 482
Cdd:TIGR02169  196 KRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  483 ELEDSLERISDQGQRKTQEQLEVLES-----------LKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL 551
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRVKEKIGELEAeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462613984  552 VSGAAHREEELSALRKELQDTQLKLASTEESMCQLAK 588
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
421-583 2.30e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. 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: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 44.16  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQN--HADLLRKNAEVTKqVSMARQAQVDLEREKKeLEDSLERISdqgqRK 498
Cdd:cd07674     20 STKELADFVRERAAIEETYSKSMSKLSKMASNgsPLGTFAPMWEVFR-VSSDKLALCHLELMRK-LNDLIKDIN----RY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  499 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaahREeelSALRKELQDTQLKLAS 578
Cdd:cd07674     94 GDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR---------RE---GVPQKELEKAELKTKK 161

                   ....*
gi 2462613984  579 TEESM 583
Cdd:cd07674    162 AAESL 166
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
347-510 1.10e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 1.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   347 LIERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAelDELRRQREDTEKAQRsls 426
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDP--TELDRAKEKLKKLLQ--- 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   427 EIERKaqaneqrysklkekyselVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERI---SDQGQRKTQEQL 503
Cdd:smart00787  219 EIMIK------------------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQL 280

                    ....*..
gi 2462613984   504 EVLESLK 510
Cdd:smart00787  281 KLLQSLT 287
 
Name Accession Description Interval E-value
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
785-983 3.70e-95

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 299.28  E-value: 3.70e-95
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   785 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 864
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   865 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 943
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462613984   944 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 983
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
12-277 6.01e-94

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: 299.21  E-value: 6.01e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   12 TVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:pfam07651    3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   91 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 169
Cdd:pfam07651   83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  170 FQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 243
Cdd:pfam07651  161 QKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  244 FYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 277
Cdd:pfam07651  240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
11-124 2.76e-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: 2.76e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   11 ETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:cd17013      1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462613984   91 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17013     81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
12-124 7.92e-69

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: 224.85  E-value: 7.92e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   12 TVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNE 91
Cdd:cd17006      2 AISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSR 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462613984   92 LSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17006     82 LKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
835-981 6.51e-60

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: 201.27  E-value: 6.51e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  835 KNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVN 914
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  915 QATAGVVASTISGKSQIEE--TDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYE 981
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
11-124 2.97e-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: 189.69  E-value: 2.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   11 ETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:cd17014      1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462613984   91 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
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; ...
12-124 1.10e-40

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: 145.60  E-value: 1.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   12 TVSINKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAVLCWKFCHVFHKLLRDGHP--NVLKDSLR- 87
Cdd:cd16986      2 EKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDa 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462613984   88 YRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd16986     81 WLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
9-131 8.04e-38

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 137.76  E-value: 8.04e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984     9 PPETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVLKDSL 86
Cdd:smart00273    1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEAL 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462613984    87 RYRNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTKMEYHTKNPRFP 131
Cdd:smart00273   81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
453-551 1.56e-34

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: 127.05  E-value: 1.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam16515    1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
                           90
                   ....*....|....*....
gi 2462613984  533 SEANWAAEFAELEKERDSL 551
Cdd:pfam16515   81 SGSQLSSQLAALQAEKEGL 99
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
13-124 2.32e-27

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: 107.39  E-value: 2.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   13 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNEL 92
Cdd:cd17007      3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462613984   93 SDMSRMW-GHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17007     83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
341-615 5.61e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.61  E-value: 5.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 419
Cdd:COG1196    219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 499
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462613984  580 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196    455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
348-615 1.84e-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: 75.09  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAeqqhlrqqaADDCEFLRAELDELRRQREDTE----KA 421
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALL---------VLRLEELREELEELQEELKEAEeeleEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLErisdQGQRKTQE 501
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----ELESKLDE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  582 SMCQLAKDQRKMLlvgsRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168  415 RRERLQQEIEELL----KKLEEAELKELQAELEE 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
342-581 2.82e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 2.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:COG1196    263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1196    343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQELATSQRELQvlqgSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:COG1196    423 LEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-593 8.73e-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: 72.78  E-value: 8.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  340 NKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDte 419
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE-- 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 kAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK-------ELEDSLERIS 492
Cdd:TIGR02168  335 -LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneieRLEARLERLE 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  493 DQGQRKTQEQLEVLESL--------KQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSlvsgAAHREEELSA 564
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA----AERELAQLQA 489
                          250       260
                   ....*....|....*....|....*....
gi 2462613984  565 LRKELQDTQLKLASTEESMCQLAKDQRKM 593
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
348-615 1.05e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQR----VVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQR 423
Cdd:COG1196    188 LERLEDILGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEE----LEAELEELEAELEELEAELA 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  424 S----LSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgqrkT 499
Cdd:COG1196    264 EleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----L 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462613984  580 EESmcQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196    420 EEE--LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
348-561 2.84e-12

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: 69.41  E-value: 2.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 427
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  428 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVD-LEREKKELEDSLERISDQGQRKtQEQLEVL 506
Cdd:COG4942    105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERAEL-EALLAEL 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462613984  507 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEE 561
Cdd:COG4942    184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-615 5.11e-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: 70.47  E-value: 5.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  353 REISGLKAQLEnmktesqrvvlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEK-AQRSLSEIERK 431
Cdd:TIGR02168  677 REIEELEEKIE-----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  432 AQANEQRYSKLKEKYSELVQNHADL--LRKNAEVTKQVSMARQAQVD-LEREKKELE---DSLERISDQGQRKTQEQLEV 505
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALRealDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  506 LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-------REEELSALRKELQDTQLKLAS 578
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRE 905
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462613984  579 TEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168  906 LESKRSELRRElEELREKLAQLELRLEGLEVRIDNLQE 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
342-610 1.59e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLkAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:COG1196    281 LELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1196    360 ---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEanwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:COG1196    437 EEEEEEALEEAAEEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462613984  582 SmcQLAKDQRKMLLVGSR-----KAAEQVIQDAL 610
Cdd:COG1196    513 A--LLLAGLRGLAGAVAVligveAAYEAALEAAL 544
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
349-659 4.15e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.40  E-value: 4.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA---- 421
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEKYSEL--------VQNHADLLRK-NAEVTKQVSMARQAQVDLER---EKKELEDSLE 489
Cdd:TIGR02169  757 KSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKlEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQ 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  490 RISDQgQRKTQEQLEvleSLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKEL 569
Cdd:TIGR02169  837 ELQEQ-RIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-------EAQLRELERKI 905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  570 QDTQLKLasteesmcqlakdQRKMLLVGSRKAAEQVIQDALNQLEEPPliscagsadhllSTVTSISSCIEQLEKSWSQY 649
Cdd:TIGR02169  906 EELEAQI-------------EKKRKRLSELKAKLEALEEELSEIEDPK------------GEDEEIPEEELSLEDVQAEL 960
                          330
                   ....*....|
gi 2462613984  650 LACPEDISGL 659
Cdd:TIGR02169  961 QRVEEEIRAL 970
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-615 2.43e-10

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: 64.69  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  340 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQlkghVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdte 419
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK----------------- 482
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieele 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  483 ----ELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRElqvlqgsletsaqseanWAAEFAELEKERDSLvsgaahr 558
Cdd:TIGR02168  866 elieELESELEALLNE-RASLEEALALLRSELEELSEELRE-----------------LESKRSELRRELEEL------- 920
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  559 EEELSALRKELQDTQLKLASTEEsmcQLAKDQRKML-----LVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLeeaeaLENKIEDDEEEARRRLKRLEN 979
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
381-602 7.76e-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: 62.09  E-value: 7.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  381 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL 456
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  457 LRKnaevtkQVSMARQAQVDLEREKKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE 534
Cdd:COG4942    110 LRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462613984  535 ANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAA 602
Cdd:COG4942    184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
406-591 1.13e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.48  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  406 AELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaEVTKQVSMARQAQVDLEREKKELE 485
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELP 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  486 DSLERIsdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLETS-AQSEANWAAEFAELEKERDSLVSGAAHREEELSA 564
Cdd:COG4717    146 ERLEEL--------EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
                          170       180
                   ....*....|....*....|....*..
gi 2462613984  565 LRKELQDTQLKLASTEESMCQLAKDQR 591
Cdd:COG4717    218 AQEELEELEEELEQLENELEAAALEER 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
405-615 1.17e-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: 62.77  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  405 RAELDELRRQredTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLERE 480
Cdd:TIGR02168  676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  481 KKELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLET--SAQSEANwaAEFAELEKERDSLVSGAAHR 558
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKAlrEALDELR--AELTLLNEEAANLRERLESL 829
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613984  559 EEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEE 615
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL------EELIEELESELEALLN 880
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
342-778 1.71e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMK------TESQRVVLQLKGHVSELEADLAEQQHLRQQaaddcefLRAELDELRRQR 415
Cdd:PRK03918   210 NEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKV 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  416 EDTEKAQ------RSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLE 489
Cdd:PRK03918   283 KELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  490 RISDQGQRKTQeqlevLESLKQELATS-----QRELQVLQGSLETSAQSEANWAAEFAELEKERDSL------------- 551
Cdd:PRK03918   363 LYEEAKAKKEE-----LERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgk 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  552 --VSGAA----HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkaaEQVIqdalnqLEEPPLISCAGSA 625
Cdd:PRK03918   438 cpVCGRElteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------EKVL------KKESELIKLKELA 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  626 DHLLSTVTSISSC-IEQLEKSWSQYLACPE-------DISGLLHSITLLAHLTSDAIAhgattCLRAPPEPADSLTEACK 697
Cdd:PRK03918   503 EQLKELEEKLKKYnLEELEKKAEEYEKLKEkliklkgEIKSLKKELEKLEELKKKLAE-----LEKKLDELEEELAELLK 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  698 QYGRETLAYLASLEEE-GSLENADSTAMRncLSKIKAIGEELLPRgLDIKQEELgDLVDKEMAATSAAIETATARIEEML 776
Cdd:PRK03918   578 ELEELGFESVEELEERlKELEPFYNEYLE--LKDAEKELEREEKE-LKKLEEEL-DKAFEELAETEKRLEELRKELEELE 653

                   ..
gi 2462613984  777 SK 778
Cdd:PRK03918   654 KK 655
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
358-548 2.15e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.32  E-value: 2.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  358 LKAQLENMKTESQRVVLQLKGHVSELEADLAE---QQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLsEIERKAQA 434
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELA 514
Cdd:COG4717    130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462613984  515 TSQRELQVLQGSLETSAQSEANWAAEFAELEKER 548
Cdd:COG4717    210 ELEEELEEAQEELEELEEELEQLENELEAAALEE 243
46 PHA02562
endonuclease subunit; Provisional
333-594 2.50e-09

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 61.18  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  333 FNSQNGVNKDekdhLIERLYREISGLKAQLENMKtesQRVVLQLKgHVSELEA----DLAEQQHLRQQAADDCEFLRAEL 408
Cdd:PHA02562   165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQ---QQIKTYNK-NIEEQRKkngeNIARKQNKYDELVEEAKTIKAEI 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  409 DELRRQREDTEKAQRSLSEIERKAQaneQRYSKLKEKYsELVQNHADLLRKNAEV---TKQVSMARQAQVDLEREKKELE 485
Cdd:PHA02562   237 EELTDELLNLVMDIEDPSAALNKLN---TAAAKIKSKI-EQFQKVIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQ 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  486 DSLERISDQgqrktQEQLEVLESlkqELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL 565
Cdd:PHA02562   313 HSLEKLDTA-----IDELEEIMD---EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
                          250       260
                   ....*....|....*....|....*....
gi 2462613984  566 RKELQDTQLKLASTEESmcqlaKDQRKML 594
Cdd:PHA02562   385 QDELDKIVKTKSELVKE-----KYHRGIV 408
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
354-615 5.00e-09

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: 60.57  E-value: 5.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  354 EISGLKAQLE---NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIER 430
Cdd:pfam01576  244 ELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  431 KaqaNEQRYSKLKEKYSELVQNH----ADLLRKNA----EVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQ 502
Cdd:pfam01576  324 K---REQEVTELKKALEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL--------QAE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  503 LEVLESLKQELATSQR----ELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:pfam01576  393 LRTLQQAKQDSEHKRKklegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462613984  579 TEEsmcQLAKDQRKMLLVGSRKAAEQVIQDAL-NQLEE 615
Cdd:pfam01576  473 TQE---LLQEETRQKLNLSTRLRQLEDERNSLqEQLEE 507
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
13-97 5.14e-09

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: 54.97  E-value: 5.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   13 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYR 89
Cdd:cd03564      3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82

                   ....*...
gi 2462613984   90 NELSDMSR 97
Cdd:cd03564     83 GHIFNLSN 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-583 6.37e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.31  E-value: 6.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  402 EFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREK 481
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  482 KELEDSLERISDQGQRKTQEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAElekERDSLVSGAAHREEE 561
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVEREL 767
                          170       180
                   ....*....|....*....|..
gi 2462613984  562 LSALRKELQDTQLKLASTEESM 583
Cdd:COG4913    768 RENLEERIDALRARLNRAEEEL 789
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
332-576 2.88e-08

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: 57.72  E-value: 2.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  332 NFNSQNGV---NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEadlaEQQHLRQQAADDCEFLRAEL 408
Cdd:TIGR04523  222 ELKKQNNQlkdNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  409 DELRRQRE---------DTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLER 479
Cdd:TIGR04523  298 SDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  480 EKKELEDSLE----RISD-----QGQRKTQEQLEV-LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 549
Cdd:TIGR04523  378 ENQSYKQEIKnlesQINDleskiQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
                          250       260
                   ....*....|....*....|....*..
gi 2462613984  550 SLVSGAAHREEELSALRKELQDTQLKL 576
Cdd:TIGR04523  458 NLDNTRESLETQLKVLSRSINKIKQNL 484
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
341-523 3.28e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHL--IERLYREISGLKAQ---LENMKT-----ESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDE 410
Cdd:COG4913    248 REQIELLepIRELAERYAAARERlaeLEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  411 LRRQR------------EDTEKAQRSLSEIERKAQANEQRYSKLK-------EKYSELVQNHADLL----RKNAEVTKQV 467
Cdd:COG4913    328 LEAQIrgnggdrleqleREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLealeEELEALEEAL 407
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462613984  468 SMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVL 523
Cdd:COG4913    408 AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
mukB PRK04863
chromosome partition protein MukB;
382-565 3.51e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 58.04  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  382 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:PRK04863   500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQVSMARQAQVDLEREKKELE----------DSLERISDQ-GQrkTQEQLEVLESLKQELATSQRELQVLQGSLETS 530
Cdd:PRK04863   576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsGE--EFEDSQDVTEYMQQLLERERELTVERDELAAR 653
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462613984  531 AQSeanwaaefaeLEKERDSLVSGAAHREEELSAL 565
Cdd:PRK04863   654 KQA----------LDEEIERLSQPGGSEDPRLNAL 678
Filament pfam00038
Intermediate filament protein;
352-570 3.68e-08

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 56.08  E-value: 3.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  352 YREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtekaqrslSEI 428
Cdd:pfam00038   53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR----------VDL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  429 ERKAQANEQRYSKLKEKYSELVqnhADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQG--------QRKTQ 500
Cdd:pfam00038  123 EAKIESLKEELAFLKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNreeaeewyQSKLE 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  501 E-QLEV------LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELE----KERDSLVSGAAHREEELSALRKEL 569
Cdd:pfam00038  200 ElQQAAarngdaLRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEM 279

                   .
gi 2462613984  570 Q 570
Cdd:pfam00038  280 A 280
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
396-614 5.99e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 5.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  396 QAADDCEFLRAELDELRRQREDTEKAQR---SLSEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAEVTKQVSMARQ 472
Cdd:COG4913    222 DTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAALRLWFAQRRLEL 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  473 AQVDLEREKKELEDSLERISDQGQRKTQEQlEVLESLKQELATSQ-RELQVLQGSLETSAQSEANWAAEFAELEKERDSL 551
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL 371
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462613984  552 VSGAAHREEELSALRKELQDTQLKLASTEESmCQLAKDQRKMLLVGSRKAAEQvIQDALNQLE 614
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEELEA-LEEALAEAEAALRDLRRELRE-LEAEIASLE 432
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
381-603 1.26e-07

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: 55.29  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  381 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEkaqRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN 460
Cdd:pfam07888   34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  461 AEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELAT---SQRELQVLQGSLETSAQSEANW 537
Cdd:pfam07888  111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeEEAERKQLQAKLQQTEEELRSL 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  538 AAEFAELEK---ERDSLVS-------------GAAHREE-ELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRK 600
Cdd:pfam07888  191 SKEFQELRNslaQRDTQVLqlqdtittltqklTTAHRKEaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270

                   ...
gi 2462613984  601 AAE 603
Cdd:pfam07888  271 QAE 273
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
334-579 1.77e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  334 NSQNGVNKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLK---GHVS-ELEADLAEQQ--HLRQQAADdcefLRAE 407
Cdd:COG3206    163 EQNLELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRqknGLVDlSEEAKLLLQQlsELESQLAE----ARAE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  408 LDELRRQREDTEKAQRSLSEIERKAQANEQrYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqVDLEREKKELEDS 487
Cdd:COG3206    235 LAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALRAQ 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  488 LERISDQGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAnwaaEFAELEKERDSLvsgaahrEEELSALRK 567
Cdd:COG3206    307 LQQEAQRILASLEAELEALQAREASL---QAQLAQLEARLAELPELEA----ELRRLEREVEVA-------RELYESLLQ 372
                          250
                   ....*....|..
gi 2462613984  568 ELQDTQLKLAST 579
Cdd:COG3206    373 RLEEARLAEALT 384
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
334-573 2.08e-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: 55.03  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  334 NSQNGVNKDEkdhlIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCE----------F 403
Cdd:TIGR04523  376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  404 LRAELDELRRQREDTEKAQRSLS-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSMARQAQVDLER 479
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  480 EKKELEDSLERISDQ----GQRKTQEQLE-VLESLKQELAtsqrELQVLQGSLEtSAQSEANwaAEFAELEKERDSLVSG 554
Cdd:TIGR04523  532 EKKEKESKISDLEDElnkdDFELKKENLEkEIDEKNKEIE----ELKQTQKSLK-KKQEEKQ--ELIDQKEKEKKDLIKE 604
                          250
                   ....*....|....*....
gi 2462613984  555 AAHREEELSALRKELQDTQ 573
Cdd:TIGR04523  605 IEEKEKKISSLEKELEKAK 623
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
404-588 3.07e-07

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: 54.69  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  404 LRAELDELRRQREDTEKAQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK 482
Cdd:TIGR02169  196 KRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  483 ELEDSLERISDQGQRKTQEQLEVLES-----------LKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL 551
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRVKEKIGELEAeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462613984  552 VSGAAHREEELSALRKELQDTQLKLASTEESMCQLAK 588
Cdd:TIGR02169  356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
347-592 3.48e-07

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: 54.57  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  347 LIERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQ-AADDCEFLRAELDELRRQREDTEKAQ 422
Cdd:COG3096    837 ELAALRQRRSELERELAQHRAQEQQLrqqLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAFIQQHG 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  423 RSLSEIERKA---QANEQRYSKLKEKYSELVQNHaDLLRKNAEVTKQVsMARQAQ------VDLEREKKELEDSLERISD 493
Cdd:COG3096    917 KALAQLEPLVavlQSDPEQFEQLQADYLQAKEQQ-RRLKQQIFALSEV-VQRRPHfsyedaVGLLGENSDLNEKLRARLE 994
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  494 QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-----REEELSALRKE 568
Cdd:COG3096    995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARirrdeLHEELSQNRSR 1074
                          250       260
                   ....*....|....*....|....
gi 2462613984  569 LQDTQLKLASTEESMCQLAKDQRK 592
Cdd:COG3096   1075 RSQLEKQLTRCEAEMDSLQKRLRK 1098
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
354-549 5.15e-07

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: 53.92  E-value: 5.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  354 EISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 433
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  434 ANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEqlevLESLKQEL 513
Cdd:TIGR02169  410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDRVEKEL 485
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462613984  514 ATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 549
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
341-532 6.92e-07

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: 53.20  E-value: 6.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHvsELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEK 420
Cdd:pfam17380  408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRslseieRKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQ 500
Cdd:pfam17380  482 EKR------DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462613984  501 EQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam17380  556 EQMRKATEERSRLEAMEREREMMRQIVESEKA 587
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
360-615 7.01e-07

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: 53.43  E-value: 7.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  360 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADdCEFLRAELDELRRQREDTEKA---------QRSLSEIER 430
Cdd:TIGR00618  229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahIKAVTQIEQ 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  431 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLevLESLK 510
Cdd:TIGR00618  308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH--IHTLQ 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  511 QELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVsgAAHREEELSALRKELQdtqlKLASTEESMCQLAKDQ 590
Cdd:TIGR00618  386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA--HAKKQQELQQRYAELC----AAAITCTAQCEKLEKI 459
                          250       260
                   ....*....|....*....|....*
gi 2462613984  591 RKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR00618  460 HLQESAQSLKEREQQLQTKEQIHLQ 484
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
382-574 7.64e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 7.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  382 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQRE------DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQN 452
Cdd:COG4913    621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAE 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLE--------------VLESLKQELATSQR 518
Cdd:COG4913    701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavereLRENLEERIDALRA 780
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  519 ELQVLQGSLEtSAQSEAN--WAAEFAEL----------EKERDSLV-SGAAHREEELSALRKELQDTQL 574
Cdd:COG4913    781 RLNRAEEELE-RAMRAFNreWPAETADLdadleslpeyLALLDRLEeDGLPEYEERFKELLNENSIEFV 848
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
403-615 8.56e-07

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: 53.15  E-value: 8.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  403 FLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSelvqnhaDLLRKNAEVTKQVSMARQaqvDLEREKK 482
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQ---EEEKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  483 ELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLETSAQSEANwaAEFAELEKERDSLVSGAAHREEEL 562
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462613984  563 SALRKELQDTQLKLASTEESMCQLakdQRKMLLVGSRKAAEQVIQDALN-QLEE 615
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIEKEIENLNgKKEE 865
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
345-614 1.08e-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: 52.81  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  345 DHLIERL---YREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:pfam15921  415 DHLRRELddrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QR-------SLSEIERKAQANEQRYSKLKE----KYSEL--VQNHADLLRkNAEV---TKQVSMARQAQVdLEREKKELE 485
Cdd:pfam15921  495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhLKNEGDHLR-NVQTeceALKLQMAEKDKV-IEILRQQIE 572
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  486 DSLERISDQGQ-------RKTQEQLEV---------LESLKQELATSQRELQVLQGSLETSAQSEANWAAE----FAELE 545
Cdd:pfam15921  573 NMTQLVGQHGRtagamqvEKAQLEKEIndrrlelqeFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIK 652
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  546 KERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMcQLAKDQRKMLLVGSRKAAEQViQDALNQLE 614
Cdd:pfam15921  653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQT-RNTLKSME 719
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-572 1.10e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  353 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAAD---DCEFLRAELDELRRQREDTEKAQRSLSEIe 429
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNE- 881
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  430 rKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELE---DSL-ERISDQGQRKTQEQLEV 505
Cdd:TIGR02168  882 -RASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLqERLSEEYSLTLEEAEAL 959
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  506 LESLKQELATSQRELQVLQGSLEtsAQSEANWAA--EFAELEKERDSLvsgaAHREEELSALRKELQDT 572
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIK--ELGPVNLAAieEYEELKERYDFL----TAQKEDLTEAKETLEEA 1022
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
347-615 1.13e-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: 52.81  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  347 LIERLYREISGLKA-------QLENMKTESQ-RVVLQLKGH-------VSELEADLAEQQHLRQQAADDCEFLRAELDEL 411
Cdd:pfam15921  225 ILRELDTEISYLKGrifpvedQLEALKSESQnKIELLLQQHqdrieqlISEHEVEITGLTEKASSARSQANSIQSQLEII 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  412 RRQ-REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQN-HADLLRKNAEVTKqvsmARQAQVDLEREKKELEDSLE 489
Cdd:pfam15921  305 QEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  490 R-ISDQGQRKTQEQLE----------------VLESLKQELATSQRELQVLQGSLET-SAQSEANWAAEFAELEKERDSL 551
Cdd:pfam15921  381 KlLADLHKREKELSLEkeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL 460
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462613984  552 vsgaahreEELSALRKELQDTQLKLASTEESMCqlakdQRKMLLvgsrKAAEQVIQDALNQLEE 615
Cdd:pfam15921  461 --------EKVSSLTAQLESTKEMLRKVVEELT-----AKKMTL----ESSERTVSDLTASLQE 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
411-615 1.22e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  411 LRRQREDTEKAQRSLSE----IERKAQANEQRYSKLKEKYS--ELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKEL 484
Cdd:COG3206    166 LELRREEARKALEFLEEqlpeLRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  485 EDSLERISDQGQRKTQEQleVLESLKQELATSQRELQVLQGSLETS-----------AQSEANWAAEFAELEKERDSLVS 553
Cdd:COG3206    246 RAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYTPNhpdvialraqiAALRAQLQQEAQRILASLEAELE 323
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  554 GAAHREEELsalRKELQDTQLKLASTEESMCQLAKDQRKmllvgsRKAAEQVIQDALNQLEE 615
Cdd:COG3206    324 ALQAREASL---QAQLAQLEARLAELPELEAELRRLERE------VEVARELYESLLQRLEE 376
PTZ00121 PTZ00121
MAEBL; Provisional
359-622 1.22e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKGHVSELEAdlAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQR 438
Cdd:PTZ00121  1406 KADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  439 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERISDQGQRKTQEQLEVLESLK-QELATSQ 517
Cdd:PTZ00121  1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAE 1561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  518 RELQVLQGSLETSAQSEANWAAEFA-ELEKERDSLVSGAAHREEELSA--LRKElQDTQLKLASTEEsmcqlAKDQRKML 594
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAeeAKKA-EEAKIKAEELKK-----AEEEKKKV 1635
                          250       260
                   ....*....|....*....|....*....
gi 2462613984  595 LVGSRKAAEQVIQ-DALNQLEEPPLISCA 622
Cdd:PTZ00121  1636 EQLKKKEAEEKKKaEELKKAEEENKIKAA 1664
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
364-606 1.44e-06

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: 52.43  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  364 NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDEL------RRQREDTEKAQRslSEIERKAQ--AN 435
Cdd:pfam17380  261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKareverRRKLEEAEKARQ--AEMDRQAAiyAE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  436 EQRYSKLKEKYSELVQNHadllrknaEVTKQVSMARQAQVDLEREKKEledSLERISDQGQRKTQEQLEVLESL-KQELA 514
Cdd:pfam17380  339 QERMAMERERELERIRQE--------ERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAArKVKIL 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  515 TSQRELQVLQGSLETS---AQSEANWAAEFAELEKER----DSLVSGAAHREEELSALRKELQDTQLK--LASTEESMCQ 585
Cdd:pfam17380  408 EEERQRKIQQQKVEMEqirAEQEEARQREVRRLEEERaremERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRK 487
                          250       260
                   ....*....|....*....|.
gi 2462613984  586 LAKDQRKMLLVGSRKAAEQVI 606
Cdd:pfam17380  488 RAEEQRRKILEKELEERKQAM 508
PTZ00121 PTZ00121
MAEBL; Provisional
359-615 1.70e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKGHVSEL-EADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRsLSEIERKAQ 433
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKK 1523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  434 ANEQRYSKLKEKYSELVQ----NHADLLRKNAEVTK--QVSMARQAQVDLER--------------EKKELEDSLERISD 493
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAKKaeekKKADELKKAEELKKaeEKKKAEEAKKAEEDknmalrkaeeakkaEEARIEEVMKLYEE 1603
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  494 QGQRKTQE-QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:PTZ00121  1604 EKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462613984  573 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
382-565 2.52e-06

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 51.88  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  382 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:COG3096    499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL-ESLKQELATSQRELQVLQGSLE---TSAQSEANW 537
Cdd:COG3096    575 EAVEQRSELRQQLEQLRARIKELAARAPA-----WLAAQDALERLrEQSGEALADSQEVTAAMQQLLErerEATVERDEL 649
                          170       180
                   ....*....|....*....|....*...
gi 2462613984  538 AAEFAELEKERDSLVSGAAHREEELSAL 565
Cdd:COG3096    650 AARKQALESQIERLSQPGGAEDPRLLAL 677
PTZ00121 PTZ00121
MAEBL; Provisional
359-615 2.60e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRSLSEIERKAQA 434
Cdd:PTZ00121  1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQA-QVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQ-- 511
Cdd:PTZ00121  1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKad 1513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  512 EL--ATSQRELQVLQGSLETSAQSEANWAAEF---------AELEKERDSLVSGAAHREEE--LSALRKELQDTQLKLAS 578
Cdd:PTZ00121  1514 EAkkAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEAR 1593
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462613984  579 TEESMcQLAKDQRKMLLVGSRKAAEQVIQ-DALNQLEE 615
Cdd:PTZ00121  1594 IEEVM-KLYEEEKKMKAEEAKKAEEAKIKaEELKKAEE 1630
PTZ00121 PTZ00121
MAEBL; Provisional
359-525 3.08e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQ--AADDCEFLRAElDELRRQREDTEKAQ--RSLSEIERKAQA 434
Cdd:PTZ00121  1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAA-EEAKKAEEDKKKAEeaKKAEEDEKKAAE 1692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ----VSMARQAQVDLEREKKELEdslERISDQGQRKTQEQLEVLESLK 510
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKK 1769
                          170
                   ....*....|....*
gi 2462613984  511 QELATSQRELQVLQG 525
Cdd:PTZ00121  1770 AEEIRKEKEAVIEEE 1784
PRK12705 PRK12705
hypothetical protein; Provisional
388-536 4.19e-06

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 50.48  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  388 AEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEvtkqv 467
Cdd:PRK12705    46 AEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELE----- 120
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  468 smarqaqvdLEREKKELEDSLERISdqGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAN 536
Cdd:PRK12705   121 ---------LEELEKQLDNELYRVA--GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAE 175
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
396-582 4.45e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  396 QAADDCEFLRAELDELRRQREDtekAQRSLSEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQV---- 467
Cdd:COG3883     13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERReelg 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  468 SMARQAQVDLER--------EKKELED------SLERISDQGQRKTQEQ---LEVLESLKQELATSQRELQVLQGSLEtS 530
Cdd:COG3883     90 ERARALYRSGGSvsyldvllGSESFSDfldrlsALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELE-A 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  531 AQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 582
Cdd:COG3883    169 AKAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
354-582 4.53e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  354 EISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 433
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  434 ANEQRYSKLKEKYSELV--QNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSlerisdqgQRKTQEQLEVLESLKQ 511
Cdd:COG3883     93 RALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAK--------KAELEAKLAELEALKA 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613984  512 ELATSQRELQvlqgsletSAQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 582
Cdd:COG3883    165 ELEAAKAELE--------AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
348-619 4.91e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 4.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVvlqlkghVSELEADLAEQQHLRQQaaddceflraeldeLRRQREDTEKAQRSLSE 427
Cdd:COG4372     40 LDKLQEELEQLREELEQAREELEQL-------EEELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQ 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  428 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQLEVLE 507
Cdd:COG4372     99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL--------QEELAALE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  508 SLKQELATSQRELQVLQgsLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLA 587
Cdd:COG4372    171 QELQALSEAEAEQALDE--LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462613984  588 KDQRKMLLVGSRKAAEQVIQDALNQLEEPPLI 619
Cdd:COG4372    249 EELLEEVILKEIEELELAILVEKDTEEEELEI 280
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
349-575 5.37e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 5.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELE------ADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQ 422
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAE----LPERLEELEERLEELRELE 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  423 RSLSEIERKAQANEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRktQE 501
Cdd:COG4717    163 EELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AA 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQEL--ATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSLVSGAAHREEELSALRKELQDTQ 573
Cdd:COG4717    241 LEERLKEARLLLliAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEE 320

                   ..
gi 2462613984  574 LK 575
Cdd:COG4717    321 LE 322
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
351-581 5.83e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.56  E-value: 5.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  351 LYREISGLKAQLENMKTESQRVVLQLKGHVSELE----ADLAEQQHLRQQAADDCEFLRAEldELRRQREDTEK--AQRS 424
Cdd:pfam01576   55 LCAEAEEMRARLAARKQELEEILHELESRLEEEEersqQLQNEKKKMQQHIQDLEEQLDEE--EAARQKLQLEKvtTEAK 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  425 LSEIERKAQANEQRYSKL-------KEKYSELVQNHADLLRKNAEVT----KQVSMARQAQVDLEREKK---ELEDS--- 487
Cdd:pfam01576  133 IKKLEEDILLLEDQNSKLskerkllEERISEFTSNLAEEEEKAKSLSklknKHEAMISDLEERLKKEEKgrqELEKAkrk 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  488 LERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWA----------AEFAE-LEKERDSLVSGAA 556
Cdd:pfam01576  213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireleaqiSELQEdLESERAARNKAEK 292
                          250       260
                   ....*....|....*....|....*...
gi 2462613984  557 HR---EEELSALRKELQDTQLKLASTEE 581
Cdd:pfam01576  293 QRrdlGEELEALKTELEDTLDTTAAQQE 320
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
385-576 5.87e-06

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: 48.77  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  385 ADLAEQQHLRQ-QAADdceflrAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK 459
Cdd:COG1579      1 AMPEDLRALLDlQELD------SELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  460 NAEVTKQVSMAR--------QAQVD-LEREKKELEDSLerisdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLEts 530
Cdd:COG1579     75 IKKYEEQLGNVRnnkeyealQKEIEsLKRRISDLEDEI-----------LELMERIEELEEELAELEAELAELEAELE-- 141
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462613984  531 aQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKELQDTQLKL 576
Cdd:COG1579    142 -EKKAELDEELAELEAELEEL-------EAEREELAAKIPPELLAL 179
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
333-643 6.02e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 6.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  333 FNSQNGVNKDEKDHLIER---LYREISGLKAQLENMK---TESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRA 406
Cdd:PRK02224   340 HNEEAESLREDADDLEERaeeLREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  407 ELDELRRQREDTEKAQRSLSEIERKAQA-------------------------NEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:PRK02224   420 ERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLE 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQVSMARQaqvdLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAA 539
Cdd:PRK02224   500 RAEDLVEAEDR----IERLEERREDLEELIAERRETieEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  540 EF----AELEKERDSL------VSGAAHREEELSALRKELQDTQL-------KLASTEESMCQLA---KDQRKMLLVGSR 599
Cdd:PRK02224   576 ELnsklAELKERIESLerirtlLAAIADAEDEIERLREKREALAElnderreRLAEKRERKRELEaefDEARIEEAREDK 655
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2462613984  600 KAAEQVIQDALNQLEEpplisCAGSADHLLSTVTSISSCIEQLE 643
Cdd:PRK02224   656 ERAEEYLEQVEEKLDE-----LREERDDLQAEIGAVENELEELE 694
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
402-613 6.93e-06

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: 50.35  E-value: 6.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  402 EFLRAELDELRRQR-EDTEKAQRSLSEIERKAQAnEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvdleRE 480
Cdd:TIGR00618  545 EDVYHQLTSERKQRaSLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL----LR 619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  481 KKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRElQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaaHREE 560
Cdd:TIGR00618  620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSIRVLPKELLASRQLALQKMQ--------SEKE 690
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462613984  561 ELSALRKELQDTQLKLASTEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 613
Cdd:TIGR00618  691 QLTYWKEMLAQCQTLLRELETHIEEYDREfNEIENASSSLGSDLAAREDALNQS 744
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
470-628 8.08e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 8.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  470 ARQAQVDLEREKKELEDSLERISDQgqrktqeqlevLESLKQELATSQRELQVLQGsLETSAQSEANWAA---EFAELEK 546
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEER-----------LEALEAELDALQERREALQR-LAEYSWDEIDVASaerEIAELEA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  547 ERDSLVSGAAhreeELSALRKELQDTQLKLASTEESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 626
Cdd:COG4913    676 ELERLDASSD----DLAALEEQLEELEAELEELEEELDELKGEIGR--LEKELEQAEEELDELQDRLEAAEDLARLELRA 749

                   ..
gi 2462613984  627 HL 628
Cdd:COG4913    750 LL 751
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
353-589 1.19e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 48.65  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  353 REISGLKAQLENMKTESQRVV---LQLKGHVSELEADLAE----QQHLRQQAADD-----CEFLRAELDELRRQREDTEK 420
Cdd:pfam15905   94 KRLQALEEELEKVEAKLNAAVrekTSLSASVASLEKQLLEltrvNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEAKMK 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqvdlerekKELEDSLERISDQGQRKT 499
Cdd:pfam15905  174 EVMAKQEgMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET--------------EKLLEYITELSCVSEQVE 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAE----LEKERDSLVSGAAHREEELSAlrkELQDTQLK 575
Cdd:pfam15905  240 KYKLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEkcklLESEKEELLREYEEKEQTLNA---ELEELKEK 315
                          250
                   ....*....|....
gi 2462613984  576 LASTEESMCQLAKD 589
Cdd:pfam15905  316 LTLEEQEHQKLQQK 329
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
380-615 1.28e-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: 49.57  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  380 VSELEADLAEQQHLRQQAADDCEFLRA-------ELDELRRQREDTekaQRSLSEIERKAQANEQRYSKLkEKYSELVQN 452
Cdd:COG3096    356 LEELTERLEEQEEVVEEAAEQLAEAEArleaaeeEVDSLKSQLADY---QQALDVQQTRAIQYQQAVQAL-EKARALCGL 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  453 hADLLRKNAEVTKQVSMARQAQVDleREKKELEDSLeRISDQGQRKTQEQLEVLESLKQELATSQ-----RELQVLQGSL 527
Cdd:COG3096    432 -PDLTPENAEDYLAAFRAKEQQAT--EEVLELEQKL-SVADAARRQFEKAYELVCKIAGEVERSQawqtaRELLRRYRSQ 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  528 ETSAQSEANWAAEFAELEKERDSL-----------------VSGAAHREEELSALRKELQDTQLKLASTEESMCQL---- 586
Cdd:COG3096    508 QALAQRLQQLRAQLAELEQRLRQQqnaerlleefcqrigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELrqql 587
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462613984  587 --AKDQRKMLlvGSRKAAEQVIQDALNQLEE 615
Cdd:COG3096    588 eqLRARIKEL--AARAPAWLAAQDALERLRE 616
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
342-583 1.32e-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: 49.05  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEAD--------------LAEQ----QHLRQQAADDCEF 403
Cdd:pfam10174  390 DVKERKINVLQKKIENLQEQLR----DKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKeriiERLKEQREREDRE 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  404 LRAELDELRRQRED---------TEKAQRSLSEIERKAQANEQRYSKLKeKYSELVQNHADLLRKNAEVTKQVSMARQAQ 474
Cdd:pfam10174  466 RLEELESLKKENKDlkekvsalqPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  475 --VDLEREKKELEDSLERISDQGQRKTQE----QLEV---LESLKQ----------------ELATSQRELQVLQGSLET 529
Cdd:pfam10174  545 naEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerlLGILREvenekndkdkkiaeleSLTLRQMKEQNKKVANIK 624
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613984  530 SAQSE--ANWAAEFAELEKERDSLVSGAAHR--EEELSAL---RKELQDTQLKLASTEESM 583
Cdd:pfam10174  625 HGQQEmkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSSTQQSL 685
mukB PRK04863
chromosome partition protein MukB;
348-604 1.54e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELeadlaeQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRS 424
Cdd:PRK04863   839 LRQLNRRRVELERALADHESQEQQQrsqLEQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRF 912
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  425 -------LSEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVsm 469
Cdd:PRK04863   913 vqqhgnaLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKL-- 990
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  470 aRQAQVDLEREKKELEDSLERISDQGQRKTQeqleVLESLKQELATSQRELQVLQGSL-ETSAQSEANwAAEFAELEKER 548
Cdd:PRK04863   991 -RQRLEQAEQERTRAREQLRQAQAQLAQYNQ----VLASLKSSYDAKRQMLQELKQELqDLGVPADSG-AEERARARRDE 1064
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462613984  549 dslvsgaahREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM--LLVGSRKAAEQ 604
Cdd:PRK04863  1065 ---------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerDYHEMREQVVN 1113
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
343-596 1.58e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.97  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  343 EKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEaDLAEQQHLRQQAADDCEFLRAELDelRRQREDTEKAQ 422
Cdd:pfam05557   94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  423 RsLSEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQR--- 497
Cdd:pfam05557  171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaat 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  498 ------KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQD 571
Cdd:pfam05557  250 lelekeKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
                          250       260
                   ....*....|....*....|....*
gi 2462613984  572 TQLKLASTEESMCQLakdQRKMLLV 596
Cdd:pfam05557  330 LNKKLKRHKALVRRL---QRRVLLL 351
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
353-578 1.88e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  353 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAadDCEFLRAELDEL-RRQREDTEKAQRSLSEIERK 431
Cdd:COG4717    319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALlAEAGVEDEEELRAALEQAEE 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  432 AQANEQRYSKLKEKyselVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKELEDSLERISDQgQRKTQEQLEVLESlKQ 511
Cdd:COG4717    397 YQELKEELEELEEQ----LEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELREE-LAELEAELEQLEE-DG 469
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613984  512 ELATSQRELQVLqgsletsaqseanwAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:COG4717    470 ELAELLQELEEL--------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAS 522
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
348-498 1.93e-05

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: 48.22  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAEQ------------QHLRQQAADDCEFLRAELDELRR 413
Cdd:COG4942     85 LAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAA 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVqnhadllrknAEVTKQVSMARQAQVDLEREKKELEDSLERISD 493
Cdd:COG4942    165 LRAELEAERAELEALLAELEEERAALEALKAERQKLL----------ARLEKELAELAAELAELQQEAEELEALIARLEA 234

                   ....*
gi 2462613984  494 QGQRK 498
Cdd:COG4942    235 EAAAA 239
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
350-569 2.56e-05

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: 48.30  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  350 RLYREISGLKAQLENMKTESQR-VVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrslseI 428
Cdd:pfam12128  657 RLFDEKQSEKDKKNKALAERKDsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----L 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  429 ERKAQANEQRYSKLKEKYSEL-VQNHADLLRKNAEvtkqvsmaRQAQVDLEREKKELEDSLERISDQGQRKT------QE 501
Cdd:pfam12128  732 ALLKAAIAARRSGAKAELKALeTWYKRDLASLGVD--------PDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyQE 803
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  502 Q-LEVLESLKQELATSQRELQVLQGSLetsAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKEL 569
Cdd:pfam12128  804 TwLQRRPRLATQLSNIERAISELQQQL---ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
383-593 2.90e-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: 48.25  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  383 LEADLAEqqhLRQQAADdcefLRAELDELRRQREDTEKA-QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:pfam01576  213 LEGESTD---LQEQIAE----LQAQIAELRAQLAKKEEElQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEsLKQELATSQR--ELQV-------------LQGS 526
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE-LKKALEEETRshEAQLqemrqkhtqaleeLTEQ 364
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462613984  527 LETSAQSEANW-------AAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM 593
Cdd:pfam01576  365 LEQAKRNKANLekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
359-663 3.19e-05

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: 48.12  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELD----ELRRQREDTEKAQRSLSEIERKAQA 434
Cdd:TIGR00606  690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEE 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  435 NEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------MARQAQVDLER-------EKKELEDSLERISDQG---Q 496
Cdd:TIGR00606  770 QETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqEKQEKQHELDTVVSKIelnR 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  497 RKTQEQLEVLESLKQELatsqRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL---RKELQDTQ 573
Cdd:TIGR00606  850 KLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetfLEKDQQEK 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  574 LKLASTEESMCQLAKDQRKML------LVGSRKAAEQVIQDalnqleeppliscaGSADHLLSTVTSISSCIEQLEKSWS 647
Cdd:TIGR00606  926 EELISSKETSNKKAQDKVNDIkekvknIHGYMKDIENKIQD--------------GKDDYLKQKETELNTVNAQLEECEK 991
                          330
                   ....*....|....*.
gi 2462613984  648 QYLACPEDISGLLHSI 663
Cdd:TIGR00606  992 HQEKINEDMRLMRQDI 1007
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
349-592 3.81e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 3.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEI 428
Cdd:PRK03918   165 KNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  429 ERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKT--- 499
Cdd:PRK03918   244 EKELESLEGSKRKLEEKIRELeerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeei 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 ---QEQLEVLES-------LKQELATSQRELQVLQGSLETSAQSEANwAAEFAELEKERDSLVSGAAHRE-EELSALRKE 568
Cdd:PRK03918   324 ngiEERIKELEEkeerleeLKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKElEELEKAKEE 402
                          250       260
                   ....*....|....*....|....
gi 2462613984  569 LQDTQLKLASTEESMCQLAKDQRK 592
Cdd:PRK03918   403 IEEEISKITARIGELKKEIKELKK 426
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
341-614 4.62e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.44  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHLIErlyrEISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHL---RQQAADDCEFLRAELDELRRQRED 417
Cdd:COG1340     28 KEKRDELNE----ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAE 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  418 TEKAQRSLSEIERKAQANEQRY-----SKLKEKysELVQNHADlLRKNAEvtkqvsmARQAQVDLEREKKELEDSLERIS 492
Cdd:COG1340    104 LNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK--ELVEKIKE-LEKELE-------KAKKALEKNEKLKELRAELKELR 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  493 DQgqrktqeqlevLESLKQELATSQRELQVLQGSLeTSAQSEANwaaefaELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:COG1340    174 KE-----------AEEIHKKIKELAEEAQELHEEM-IELYKEAD------ELRKEADELHKEIVEAQEKADELHEEIIEL 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462613984  573 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLE 614
Cdd:COG1340    236 QKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
349-615 4.64e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.74  E-value: 4.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREisgLKAQLENMKTESQRVVLQLKghVSELE-------ADLAEQQHLRQQAADDCEFLRAELDELRRQREDtekA 421
Cdd:PRK10929    78 PKLSAE---LRQQLNNERDEPRSVPPNMS--TDALEqeilqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE---A 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEkyselvqnhADLLRKNAEVTkqvsmARQAQVDlerekkELEdsLERIS-DQGQRKTQ 500
Cdd:PRK10929   150 RRQLNEIERRLQTLGTPNTPLAQ---------AQLTALQAESA-----ALKALVD------ELE--LAQLSaNNRQELAR 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  501 EQLEVLESLKQELatsQRELQVLQGSLETSAQSEANWAAEFAE-LEKERDSL---VSGAAHREEELSALrkelqdtqlkl 576
Cdd:PRK10929   208 LRSELAKKRSQQL---DAYLQALRNQLNSQRQREAERALESTElLAEQSGDLpksIVAQFKINRELSQA----------- 273
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462613984  577 asteesmcqLAKDQRKMLLVGS--RKAAEQVIQ--DALNQLEE 615
Cdd:PRK10929   274 ---------LNQQAQRMDLIASqqRQAASQTLQvrQALNTLRE 307
PLN02939 PLN02939
transferase, transferring glycosyl groups
358-551 6.50e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 47.20  E-value: 6.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  358 LKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQR-------SLSEIER 430
Cdd:PLN02939   199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  431 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL 506
Cdd:PLN02939   279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKE-----ANVSKFSSYKV 353
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462613984  507 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSL 551
Cdd:PLN02939   354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTlsklkeESKKRSL 404
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-561 9.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 9.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHLIERLYREISGLKAQLENMKTESqrvVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEK 420
Cdd:PRK03918   558 LAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDK 630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQ--RK 498
Cdd:PRK03918   631 AFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEerEK 708
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613984  499 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE-ANWAAE-FAELEKERdslVSGAAHREEE 561
Cdd:PRK03918   709 AKKELEKLEKALERVEELREKVKKYKALLKERALSKvGEIASEiFEELTEGK---YSGVRVKAEE 770
PTZ00121 PTZ00121
MAEBL; Provisional
339-512 9.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 9.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  339 VNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAeqqhlRQQAADDCEFLRaELDELR-----R 413
Cdd:PTZ00121  1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKkaeekK 1290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERiSD 493
Cdd:PTZ00121  1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEK-AE 1367
                          170
                   ....*....|....*....
gi 2462613984  494 QGQRKTQEQLEVLESLKQE 512
Cdd:PTZ00121  1368 AAEKKKEEAKKKADAAKKK 1386
PTZ00121 PTZ00121
MAEBL; Provisional
359-615 1.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQLKghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSlseieRKAQANEQR 438
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKK 1634
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  439 YSKLKEKYSELVQNhADLLRKNAEVT--KQVSMARQAqvdlEREKKELEDSleRISDQGQRKTQEQlevlesLKQELATS 516
Cdd:PTZ00121  1635 VEQLKKKEAEEKKK-AEELKKAEEENkiKAAEEAKKA----EEDKKKAEEA--KKAEEDEKKAAEA------LKKEAEEA 1701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  517 QRELQVLQGSLEtsaqsEANWAAEFAELEKERDSLVSGAAHREEElsalrKELQDTQLKLASTEESMCQLAKDQRKMLLV 596
Cdd:PTZ00121  1702 KKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
                          250
                   ....*....|....*....
gi 2462613984  597 GSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDE 1790
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
419-610 1.35e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  419 EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrK 498
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----S 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  499 TQEQLEVLEslkQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQdtQLKLAS 578
Cdd:COG4372    106 LQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAE 180
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462613984  579 TEESMCQLAKDQRKMLLVGSRKAAEQVIQDAL 610
Cdd:COG4372    181 AEQALDELLKEANRNAEKEEELAEAEKLIESL 212
PTZ00121 PTZ00121
MAEBL; Provisional
332-615 1.42e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  332 NFNSQNGVNKDEKDHLIERLYREISGLKAQlENMKTESQRVVLQLKGHvseleadlAEQQHLRQQAADDCEFLRAELDEL 411
Cdd:PTZ00121  1264 HFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKK--------AEEAKKADEAKKKAEEAKKKADAA 1334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  412 RRQREDTEKAQRSlSEIERKAQANEQRYSKLKEKYSEL----VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDS 487
Cdd:PTZ00121  1335 KKKAEEAKKAAEA-AKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  488 LE--RISDQGQRKTQEQLEVLESLKQelATSQRELQVLQGSLETSAQSE-----------ANWAAEFAELEKERDSLVSG 554
Cdd:PTZ00121  1414 AAakKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEeakkkaeeakkADEAKKKAEEAKKADEAKKK 1491
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613984  555 AAHREEELSALRKELQDT----QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121  1492 AEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
351-506 1.44e-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: 46.10  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  351 LYREISGLKAQLENmktesqrvVLQLKGHVSELEADLAEQQHLRQQAADDC----------EFLRAELDELRRQREDTEK 420
Cdd:COG3096    500 LLRRYRSQQALAQR--------LQQLRAQLAELEQRLRQQQNAERLLEEFCqrigqqldaaEELEELLAELEAQLEELEE 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSE----IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEV------TKQVSMARQAQVDLEREKKELEDSLEr 490
Cdd:COG3096    572 QAAEAVEqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadSQEVTAAMQQLLEREREATVERDELA- 650
                          170
                   ....*....|....*.
gi 2462613984  491 isdQGQRKTQEQLEVL 506
Cdd:COG3096    651 ---ARKQALESQIERL 663
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
341-579 1.51e-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: 45.88  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  341 KDEKDHLIERLYREISGL---KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELdelRRQRED 417
Cdd:pfam15921  613 KDKKDAKIRELEARVSDLeleKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSEE 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  418 TEKAQRSLSEIERKAQAN-EQRYSKLKEKysELVQNHAdlLRKNAEVTKQVSmARQAQVD-LEREKKELEDSLERISDQG 495
Cdd:pfam15921  690 METTTNKLKMQLKSAQSElEQTRNTLKSM--EGSDGHA--MKVAMGMQKQIT-AKRGQIDaLQSKIQFLEEAMTNANKEK 764
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  496 QRKTQEQlevlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSalRKELQDTQLK 575
Cdd:pfam15921  765 HFLKEEK----NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ--RQEQESVRLK 838

                   ....
gi 2462613984  576 LAST 579
Cdd:pfam15921  839 LQHT 842
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
417-580 1.64e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 45.11  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  417 DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLEREKKELED--S 487
Cdd:pfam00529   52 DPTDYQAALDSAEaqlAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQaavkAAQAQLAQAQIDLARrrV 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  488 LERISDQGQRKTQEQLEVLESLKQELATSQRELqvlqgsletsAQSEANWAAEFAELEKERDSLVSGAahrEEELSALRK 567
Cdd:pfam00529  132 LAPIGGISRESLVTAGALVAQAQANLLATVAQL----------DQIYVQITQSAAENQAEVRSELSGA---QLQIAEAEA 198
                          170
                   ....*....|...
gi 2462613984  568 ELQDTQLKLASTE 580
Cdd:pfam00529  199 ELKLAKLDLERTE 211
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
348-573 1.65e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 45.06  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQ----QAADDCEFLRAELDELRRQREDTEKAQR 423
Cdd:pfam19220   74 LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEalerQLAAETEQNRALEEENKALREEAQAAEK 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  424 SLSEIERKAQANEQRYS-------KLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgq 496
Cdd:pfam19220  154 ALQRAEGELATARERLAlleqenrRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ-- 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  497 rktqeQLEVLESLKQELATSQRELQVLQGSLETSAQ------------SEANWAAE--FAELEKERDSLVSGAAHREEEL 562
Cdd:pfam19220  232 -----LEEAVEAHRAERASLRMKLEALTARAAATEQllaearnqlrdrDEAIRAAErrLKEASIERDTLERRLAGLEADL 306
                          250
                   ....*....|.
gi 2462613984  563 SALRKELQDTQ 573
Cdd:pfam19220  307 ERRTQQFQEMQ 317
PRK12704 PRK12704
phosphodiesterase; Provisional
359-536 1.67e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  359 KAQLENMKTESQRVVLQlkghvSELEADLAEQQHLRQQaaddceflRAELDELRRQREDtEKAQRsLSEIERKAQANEQR 438
Cdd:PRK12704    30 EAKIKEAEEEAKRILEE-----AKKEAEAIKKEALLEA--------KEEIHKLRNEFEK-ELRER-RNELQKLEKRLLQK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  439 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqRKTQEQL--EVLESLKQELats 516
Cdd:PRK12704    95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS----GLTAEEAkeILLEKVEEEA--- 167
                          170       180
                   ....*....|....*....|
gi 2462613984  517 QRELQVLQGSLETSAQSEAN 536
Cdd:PRK12704   168 RHEAAVLIKEIEEEAKEEAD 187
mukB PRK04863
chromosome partition protein MukB;
360-626 1.67e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  360 AQLENMKTESQRVVLQLkghvSELEADLAEQQHLRQQA------------ADDCEflrAELDELRRQREDtekAQRSLSE 427
Cdd:PRK04863   786 KRIEQLRAEREELAERY----ATLSFDVQKLQRLHQAFsrfigshlavafEADPE---AELRQLNRRRVE---LERALAD 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  428 IERKAQANEQRYSKLKEKYSEL--VQNHADLLRKN------AEVTKQVSMARQAQVDLEREKKELEdSLERIsdqgQRKT 499
Cdd:PRK04863   856 HESQEQQQRSQLEQAKEGLSALnrLLPRLNLLADEtladrvEEIREQLDEAEEAKRFVQQHGNALA-QLEPI----VSVL 930
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  500 QEQLEVLESLKQELATSQRELQVLQG---SLETSAQSEANWA-AEFAELEKERDSLVSGAAHREEELSALRKElQDTQLK 575
Cdd:PRK04863   931 QSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTR-AREQLR 1009
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  576 lasteESMCQLAK-DQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 626
Cdd:PRK04863  1010 -----QAQAQLAQyNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
348-511 1.80e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtEKAQRS 424
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRREL---EELREK 923
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  425 LSEIERKAQANEQRYSKLKEKYSELVQ-NHADLLRKNAEVTKQVSMARQAQVDLEREKKEL----EDSLERISDQGQRK- 498
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYd 1003
                          170
                   ....*....|....*
gi 2462613984  499 --TQEQLEVLESLKQ 511
Cdd:TIGR02168 1004 flTAQKEDLTEAKET 1018
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
385-578 1.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  385 ADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQAneqRYSKLKEKYSELVQNHADLLRKNAEVT 464
Cdd:COG1196    588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR---RAVTLAGRLREVTLEGEGGSAGGSLTG 664
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  465 KQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL 544
Cdd:COG1196    665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462613984  545 EKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:COG1196    745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
348-603 2.08e-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: 45.02  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLA-----------EQQHLRQQAA-DDCEFLRAELDELR 412
Cdd:pfam05701   72 LESTKRLIEELKLNLERAQTEEAQAKQDSelaKLRVEEMEQGIAdeasvaakaqlEVAKARHAAAvAELKSVKEELESLR 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  413 RQRED--------TEKAQRSLS---EIERKAQANEQRYSKLKEkysELVQNHADLLrkNAEVTK-QVSMAR-QAQVDLER 479
Cdd:pfam05701  152 KEYASlvserdiaIKRAEEAVSaskEIEKTVEELTIELIATKE---SLESAHAAHL--EAEEHRiGAALAReQDKLNWEK 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  480 EKKELEDSLERISDQ------GQRKTQEQLEVLESLKQEL-----------------------------ATSQRELQVLQ 524
Cdd:pfam05701  227 ELKQAEEELQRLNQQllsakdLKSKLETASALLLDLKAELaaymesklkeeadgegnekktstsiqaalASAKKELEEVK 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  525 GSLEtSAQSEANW---AAEF--AELEKERDSLVS----------GAAHREEELSALRKELQDTQLKLASTEESMCQLAkd 589
Cdd:pfam05701  307 ANIE-KAKDEVNClrvAAASlrSELEKEKAELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELP-- 383
                          330
                   ....*....|....
gi 2462613984  590 qrKMLLVGSRKAAE 603
Cdd:pfam05701  384 --KQLQQAAQEAEE 395
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
421-583 2.30e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. 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: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 44.16  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQN--HADLLRKNAEVTKqVSMARQAQVDLEREKKeLEDSLERISdqgqRK 498
Cdd:cd07674     20 STKELADFVRERAAIEETYSKSMSKLSKMASNgsPLGTFAPMWEVFR-VSSDKLALCHLELMRK-LNDLIKDIN----RY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  499 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaahREeelSALRKELQDTQLKLAS 578
Cdd:cd07674     94 GDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR---------RE---GVPQKELEKAELKTKK 161

                   ....*
gi 2462613984  579 TEESM 583
Cdd:cd07674    162 AAESL 166
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
387-615 2.34e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  387 LAEQQHLRQQAADDCEfLRAELDELRRQREDTEKAQRSLSEIERKAQANEqryskLKEKYSELVQNHADLLRKNAEVTKQ 466
Cdd:COG4717    293 LAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDLSPEELLE-----LLDRIEELQELLREAEELEEELQLE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  467 VSMARQAQVdLEREKKELEDSLERISDQGQRKtQEQLEVLESLKQELATSQRELQVLQgsletSAQSEANWAAEFAELEk 546
Cdd:COG4717    367 ELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELE- 438
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  547 erdslvsgaahreEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkAAEQVIQDALNQLEE 615
Cdd:COG4717    439 -------------EELEELEEELEELREELAELEAELEQLEEDGELA-------ELLQELEELKAELRE 487
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
342-513 2.54e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMKTEsqrvVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdteka 421
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE----- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSmarQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1579     91 ---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAE 164
                          170
                   ....*....|..
gi 2462613984  502 QLEVLESLKQEL 513
Cdd:COG1579    165 REELAAKIPPEL 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
482-643 2.59e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  482 KELEDSLERISDQGQRKTQ---EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL--VSGAA 556
Cdd:COG4717     49 ERLEKEADELFKPQGRKPElnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  557 HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSIS 636
Cdd:COG4717    129 PLYQELEALEAELAELPERLEELEERLEELRELEEEL------EELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                   ....*..
gi 2462613984  637 SCIEQLE 643
Cdd:COG4717    203 ELQQRLA 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
349-615 2.62e-04

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: 44.81  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREISGLKAQLENMKT--ESQRvvlQLKGHVSELEADLAEQQHLRQQAADDCEflraELDELRRQredTEKAQRSLS 426
Cdd:pfam10174  126 ERQAKELFLLRKTLEEMELriETQK---QTLGARDESIKKLLEMLQSKGLPKKSGE----EDWERTRR---IAEAEMQLG 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  427 EIERKAQANEQRYSKLKEKYSELVQNHADllRKNAEVTKQVSMARQAQV-DLEREKKELEDSLERISDQGQRKTQE---- 501
Cdd:pfam10174  196 HLEVLLDQKEKENIHLREELHRRNQLQPD--PAKTKALQTVIEMKDTKIsSLERNIRDLEDEVQMLKTNGLLHTEDreee 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 --QLEV-----------LESLKQELATSQRELQVLQGSLET--SAQSEANWAAEF------------AELEKERDSLVSG 554
Cdd:pfam10174  274 ikQMEVykshskfmknkIDQLKQELSKKESELLALQTKLETltNQNSDCKQHIEVlkesltakeqraAILQTEVDALRLR 353
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462613984  555 AAHREEELSALRKELQDTqlklasTEESMCQLA--KDQRKMLLVGSRKAaeQVIQDALNQLEE 615
Cdd:pfam10174  354 LEEKESFLNKKTKQLQDL------TEEKSTLAGeiRDLKDMLDVKERKI--NVLQKKIENLQE 408
PRK11637 PRK11637
AmiB activator; Provisional
368-547 2.73e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  368 ESQRVVLQLKGHVSELEADLAeqqHLRQQAADDCEFLRAELDELRRQ-----------REDTEKAQRSLSEIERKAQANE 436
Cdd:PRK11637    93 ETQNTLNQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsGEESQRGERILAYFGYLNQARQ 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  437 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLE-----REK--KELEDSLERisDQGQRKTQEQLEVleSL 509
Cdd:PRK11637   170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEqarneRKKtlTGLESSLQK--DQQQLSELRANES--RL 245
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462613984  510 KQELATSQRELQvlqgsleTSAQSEANWAAEFAELEKE 547
Cdd:PRK11637   246 RDSIARAEREAK-------ARAEREAREAARVRDKQKQ 276
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
442-613 3.40e-04

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: 44.50  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  442 LKEKYSELVQNHADLLRKNAEVTKQVSMARQ----AQVDLEREKKELEDSLERISDQGQRKTQEQlevleslkQELATSQ 517
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKErykrDREQWERQRRELESRVAELKEELRQSREKH--------EELEEKY 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  518 RELQVLQGSL--ETSAQSEANWA--AEFAELEKERDSLVSGAAHREEELS----------ALRKELQ----DTQLKLAST 579
Cdd:pfam07888  104 KELSASSEELseEKDALLAQRAAheARIRELEEDIKTLTQRVLERETELErmkerakkagAQRKEEEaerkQLQAKLQQT 183
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462613984  580 EESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 613
Cdd:pfam07888  184 EEELRSLSKEfQELRNSLAQRDTQVLQLQDTITTL 218
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
356-615 4.33e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  356 SGLKAQLEnmKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKA 432
Cdd:PRK02224   190 DQLKAQIE--EKEEKDLHERLNGLeseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  433 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESL 509
Cdd:PRK02224   268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleECRVAAQAHNEEAESL 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  510 KQELATsqrelqvlqgsLETSAQsEANWAAefAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAkD 589
Cdd:PRK02224   348 REDADD-----------LEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-D 412
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462613984  590 QRKML------LVGSRKAAEQVIQDALNQLEE 615
Cdd:PRK02224   413 FLEELreerdeLREREAELEATLRTARERVEE 444
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
506-644 5.34e-04

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: 43.21  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  506 LESLKQELAT-SQRELQVLQ-----------GSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQ 573
Cdd:pfam09787    2 LESAKQELADyKQKAARILQskekliaslkeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613984  574 LKLASTEESMCQLAKDQRKMLLvgSRKAAEQVIQDALNQLEEppliSCAGSADHLLSTVTSISSCIEQLEK 644
Cdd:pfam09787   82 AQQQEEAESSREQLQELEEQLA--TERSARREAEAELERLQE----ELRYLEEELRRSKATLQSRIKDREA 146
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
343-615 5.43e-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: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  343 EKDHLIERLYREISGLKAQLENMKTESQRVvLQLKGHVSELEADLAEQQHLRQqaaddcEFLRAELDELRRQREDTEKAQ 422
Cdd:TIGR00618  567 EIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALL------RKLQPEQDLQDVRLHLQQCSQ 639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  423 R-SLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN-AEVTKQVSMARQAQVDLE--REKKELEDSLERISDQGQRK 498
Cdd:TIGR00618  640 ElALKLTALHALQLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDRE 719
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  499 TQEQLEVLESLKQELATSQRELQVLQGSLetsaQSEANWAAEFAELEKERDSLVSGA--------AHREEELSALRKELQ 570
Cdd:TIGR00618  720 FNEIENASSSLGSDLAAREDALNQSLKEL----MHQARTVLKARTEAHFNNNEEVTAalqtgaelSHLAAEIQFFNRLRE 795
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462613984  571 DTQLKLASTEESMCQLAKDQRKMLLVGSRKAAeQVIQDALNQLEE 615
Cdd:TIGR00618  796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEE 839
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
343-582 7.72e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  343 EKDHLIERLYREISGLKaQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQ 422
Cdd:PRK03918   142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  423 RSLSEIERkaqaNEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDqgQRKTQEQ 502
Cdd:PRK03918   221 EELEKLEK----EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEKAEE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  503 LEVLESLKQELATSQRELQVLQGSLEtsaqseanwaAEFAELEKERDSLVSgaahREEELSALRKELQDTQLKLASTEES 582
Cdd:PRK03918   295 YIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEER 360
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
334-572 7.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  334 NSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRR 413
Cdd:COG1196    580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD 493
Cdd:COG1196    660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  494 QGQRKTQEQLEV----------LESLKQELATSQRELQVLqGSLetsaqseaNWAA--EFAELEKERDSLVSgaahREEE 561
Cdd:COG1196    740 ELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL-GPV--------NLLAieEYEELEERYDFLSE----QRED 806
                          250
                   ....*....|.
gi 2462613984  562 LSALRKELQDT 572
Cdd:COG1196    807 LEEARETLEEA 817
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
389-604 8.36e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 8.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  389 EQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK--- 465
Cdd:pfam02463  181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQ--LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskq 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  466 --QVSMARQAQVDLEREKKELEDSL-ERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFA 542
Cdd:pfam02463  259 eiEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  543 ELEKERDSLVSGAAHREEELSALRKElqdtQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQ 604
Cdd:pfam02463  339 ELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
466-615 9.34e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  466 QVSMARQAQVDLEREKKELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQseanwaaEFAELE 545
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELE 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613984  546 KERDSLVSGAAHREEELSALRKELQ----DTQLKLASTEESMCQLAKDQRKM-LLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAA 164
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
343-593 1.02e-03

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: 43.18  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  343 EKDHLIERLyreisglKAQLENMktesqrvvLQLKG-HVSELEADLAEQQHLRQQAADDceflRAELDELRRQREdteKA 421
Cdd:pfam15921  559 EKDKVIEIL-------RQQIENM--------TQLVGqHGRTAGAMQVEKAQLEKEINDR----RLELQEFKILKD---KK 616
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:pfam15921  617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKE---LQDTQLKLAs 578
Cdd:pfam15921  697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLS- 775
                          250
                   ....*....|....*
gi 2462613984  579 teESMCQLAKDQRKM 593
Cdd:pfam15921  776 --QELSTVATEKNKM 788
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
368-533 1.05e-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: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  368 ESQRVVLQLkghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLK 443
Cdd:COG1579      4 EDLRALLDL----QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAktelEDLEKEIKRLELEIEEVEARIKKYE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  444 EKYSElVQNH---ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQREL 520
Cdd:COG1579     80 EQLGN-VRNNkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
                          170
                   ....*....|...
gi 2462613984  521 QVLQGSLETSAQS 533
Cdd:COG1579    159 EELEAEREELAAK 171
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
409-615 1.08e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 43.22  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  409 DELRRQREDTEKAQRSLS----EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKEL 484
Cdd:pfam18971  610 DEVKKAQKDLEKSLRKREhlekEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQ-NLKGIKREL 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  485 EDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSeANWAAEFAELEKERDSLVSGAAHREEELSA 564
Cdd:pfam18971  689 SDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQ 767
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613984  565 LRKELQDT------QLKLASTEESMCQLAKDQRKMllvGSRKAAEQVIQDALNQLEE 615
Cdd:pfam18971  768 AKSDLENSvkdviiNQKVTDKVDNLNQAVSVAKAM---GDFSRVEQVLADLKNFSKE 821
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
342-583 1.09e-03

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: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMKTEsqrvvlqlkghVSELEADLAEQQHLRQQAADDCEFlrAELDEL-RRQREDTEK 420
Cdd:COG5185    271 GENAESSKRLNENANNLIKQFENTKEK-----------IAEYTKSIDIKKATESLEEQLAAA--EAEQELeESKRETETG 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHAdlLRKNAEvtkqvsmarqaqvDLEREKKELEDSLERISDQGQRKTQ 500
Cdd:COG5185    338 IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE--LSKSSE-------------ELDSFKDTIESTKESLDEIPQNQRG 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  501 EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKE-----RDSLVSGAAHREEELSALRKELQDTQLK 575
Cdd:COG5185    403 YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvmREADEESQSRLEEAYDEINRSVRSKKED 482

                   ....*...
gi 2462613984  576 LASTEESM 583
Cdd:COG5185    483 LNEELTQI 490
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
347-510 1.10e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 1.10e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   347 LIERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAelDELRRQREDTEKAQRsls 426
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDP--TELDRAKEKLKKLLQ--- 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984   427 EIERKaqaneqrysklkekyselVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERI---SDQGQRKTQEQL 503
Cdd:smart00787  219 EIMIK------------------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQL 280

                    ....*..
gi 2462613984   504 EVLESLK 510
Cdd:smart00787  281 KLLQSLT 287
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
344-522 1.17e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  344 KDHLIERLYREISGLKAQLENM--KTESQRVvlqlkghvsELEADLAEQQHLRQQAaddceflraeldelRRQREDTEKA 421
Cdd:PRK00409   500 PENIIEEAKKLIGEDKEKLNELiaSLEELER---------ELEQKAEEAEALLKEA--------------EKLKEELEEK 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  422 QRSLSEIERKAqaneqrYSKLKEKYSELVQNhadlLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrktqE 501
Cdd:PRK00409   557 KEKLQEEEDKL------LEEAEKEAQQAIKE----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLN--------K 618
                          170       180
                   ....*....|....*....|.
gi 2462613984  502 QLEVLESLKQELATSQRELQV 522
Cdd:PRK00409   619 ANEKKEKKKKKQKEKQEELKV 639
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
370-470 1.21e-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: 42.44  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  370 QRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEK 445
Cdd:COG4942    142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQE 221
                           90       100
                   ....*....|....*....|....*
gi 2462613984  446 YSELVQNHADLLRKNAEVTKQVSMA 470
Cdd:COG4942    222 AEELEALIARLEAEAAAAAERTPAA 246
mukB PRK04863
chromosome partition protein MukB;
382-615 1.22e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  382 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLkEKYSElvqnhaDLLRKNA 461
Cdd:PRK04863   290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQA------DLEELEE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  462 EVTKQvSMARQaqvdlerEKKELEDSLERisdqgqRKTQEQLEVLEsLKQELATSQRELQVLQgsLETSAQSEANWAAEF 541
Cdd:PRK04863   363 RLEEQ-NEVVE-------EADEQQEENEA------RAEAAEEEVDE-LKSQLADYQQALDVQQ--TRAIQYQQAVQALER 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  542 AELEKERDSL-VSGAAHREEELSALRKELQDTQLKLAsTEESMCQLAKDQ--RKMLLVG------SRKAAEQVIQDALNQ 612
Cdd:PRK04863   426 AKQLCGLPDLtADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQfeQAYQLVRkiagevSRSEAWDVARELLRR 504

                   ...
gi 2462613984  613 LEE 615
Cdd:PRK04863   505 LRE 507
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
342-615 1.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  342 DEKDHLIERLYREISGLKAQLENMKTESQrvvlQLKGHVSELEADLAEQQHLR------------------------QQA 397
Cdd:PRK03918   448 EHRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIklkelaeqlkeleeklkkynleelEKK 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  398 ADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsmarqaqvDL 477
Cdd:PRK03918   524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  478 EREKKELEDSLER---ISDQGQRKtQEQLEVLESLKQELATSQRELQVLQGSLEtSAQSEANWAA------EFAELEKER 548
Cdd:PRK03918   591 EERLKELEPFYNEyleLKDAEKEL-EREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEkkyseeEYEELREEY 668
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  549 DSLvsgaahrEEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsRKAAEQV--IQDALNQLEE 615
Cdd:PRK03918   669 LEL-------SRELAGLRAELEELEKRREEIKKTLEKLKEELEER-----EKAKKELekLEKALERVEE 725
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
406-575 1.54e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.96  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  406 AELDElRRQREDTEKAQRSLSEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtkqvsmaRQAQVDLEREKKELE 485
Cdd:COG1566     74 ARLDP-TDLQAALAQAEAQLAA----AEAQLARLEAELGAEAEIAAAEAQLAAAQAQL-------DLAQRELERYQALYK 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  486 DSLerISDQgqrktqeqleVLESLKQELATSQRELQVLQGSLEtSAQSEANWAAEFAELEKERDSLvsgaahrEEELSAL 565
Cdd:COG1566    142 KGA--VSQQ----------ELDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQVAQA-------EAALAQA 201
                          170
                   ....*....|
gi 2462613984  566 RKELQDTQLK 575
Cdd:COG1566    202 ELNLARTTIR 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
432-614 1.59e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  432 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKTQEQLEVLESLKQ 511
Cdd:TIGR02168  632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRK 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  512 ELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEEsmcQLAKDQR 591
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE---ELAEAEA 782
                          170       180
                   ....*....|....*....|...
gi 2462613984  592 KmllvgsRKAAEQVIQDALNQLE 614
Cdd:TIGR02168  783 E------IEELEAQIEQLKEELK 799
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
349-614 1.65e-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: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  349 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEF--------LRAELDELRRQREDTEK 420
Cdd:pfam12128  386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQ 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSMARQAQVD--------------------LERE 480
Cdd:pfam12128  466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  481 KKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHR 558
Cdd:pfam12128  544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613984  559 EEELSALRKELQDTQLKLA-------STEESMCQLAKDQR--KMLLVGSRKAAEQVIQDALNQLE 614
Cdd:pfam12128  624 EEQLVQANGELEKASREETfartalkNARLDLRRLFDEKQseKDKKNKALAERKDSANERLNSLE 688
mukB PRK04863
chromosome partition protein MukB;
348-560 1.70e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKtesQRV-----VLQLKGHVSELEA--DLAEQQHLRQQaaddcefLRAELDELRRQREdteK 420
Cdd:PRK04863   937 FEQLKQDYQQAQQTQRDAK---QQAfalteVVQRRAHFSYEDAaeMLAKNSDLNEK-------LRQRLEQAEQERT---R 1003
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV--SMARQAQVDLEREKKELEDSLERISDQGQRK 498
Cdd:PRK04863  1004 AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdsGAEERARARRDELHARLSANRSRRNQLEKQL 1083
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613984  499 TQEQLEvLESLKQELATSQRELQVLQgslETSAQSEANWaaeFAELEKERDSLVSGAAHREE 560
Cdd:PRK04863  1084 TFCEAE-MDNLTKKLRKLERDYHEMR---EQVVNAKAGW---CAVLRLVKDNGVERRLHRRE 1138
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
403-570 1.98e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.04  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  403 FLRAELDELRRQREDTEKAQ-RSLSEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNaEVTKQVSMarQAQVDLEREK 481
Cdd:pfam05557    6 ESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQEL-QKRIRLLEKR-EAEAEEAL--REQAELNRLK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  482 KELEDSLERISDQGQRKTQEQLEVLESLKQELA--------------TSQRELQVLQGSLETSAQSEANWAAEFAELEKE 547
Cdd:pfam05557   82 KKYLEALNKKLNEKESQLADAREVISCLKNELSelrrqiqraelelqSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
                          170       180
                   ....*....|....*....|...
gi 2462613984  548 RDSLvsgaAHREEELSALRKELQ 570
Cdd:pfam05557  162 QSSL----AEAEQRIKELEFEIQ 180
Filament pfam00038
Intermediate filament protein;
337-523 2.06e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  337 NGVNKDEKDHLIER--LYREISGLKAQLENMKTESQRVVLQLKGHVSEleadlaEQQHLRQQAADDCEFLRAeLDELRRQ 414
Cdd:pfam00038  106 VGLRKDLDEATLARvdLEAKIESLKEELAFLKKNHEEEVRELQAQVSD------TQVNVEMDAARKLDLTSA-LAEIRAQ 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  415 REdtEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNH----ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLER 490
Cdd:pfam00038  179 YE--EIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAkeeiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462613984  491 ISDQGQRKTQEQLEVLESLKQELATSQRELQVL 523
Cdd:pfam00038  257 QLADYQELISELEAELQETRQEMARQLREYQEL 289
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
347-615 2.47e-03

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.66  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  347 LIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQ---QHLRQQAADD-----------CEFLRAELDEL- 411
Cdd:pfam07111  307 LLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQsqeQAILQRALQDkaaevevermsAKGLQMELSRAq 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  412 ---RRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS-----MARQ---AQVDLE-- 478
Cdd:pfam07111  387 earRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglMARKvalAQLRQEsc 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  479 ---------------------REKKELEDSLE-----------RISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGS 526
Cdd:pfam07111  467 pppppappvdadlsleleqlrEERNRLDAELQlsahliqqevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQ 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  527 LETSAQSEANWAAEFAELEKE--RDSLVSGAAHRE---EELSALRKELQDTQLKLastEESMCQLAKDQRKMLLVGSRKA 601
Cdd:pfam07111  547 LEVARQGQQESTEEAASLRQEltQQQEIYGQALQEkvaEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAT 623
                          330
                   ....*....|....
gi 2462613984  602 AEQVIQDALNQLEE 615
Cdd:pfam07111  624 QEKERNQELRRLQD 637
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
405-520 2.55e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  405 RAELDE-LRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKE 483
Cdd:pfam20492    8 KQELEErLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE 87
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462613984  484 LEDSLERISDQGQRKTQEQlevlESLKQELATSQREL 520
Cdd:pfam20492   88 AQEEIARLEEEVERKEEEA----RRLQEELEEAREEE 120
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
336-615 3.04e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  336 QNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQR 415
Cdd:pfam01576  370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  416 EDTEK------------------AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDL 477
Cdd:pfam01576  450 NEAEGkniklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  478 EREKKELEDSLERIsDQGQRKTQEQLEVL------------------ESLKQEL------ATSQRE----LQVLQGSLET 529
Cdd:pfam01576  530 KKKLEEDAGTLEAL-EEGKKRLQRELEALtqqleekaaaydklektkNRLQQELddllvdLDHQRQlvsnLEKKQKKFDQ 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  530 SAQSEANWAAEFAElekERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKML------------LVG 597
Cdd:pfam01576  609 MLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgknvheLER 685
                          330
                   ....*....|....*...
gi 2462613984  598 SRKAAEQVIQDALNQLEE 615
Cdd:pfam01576  686 SKRALEQQVEEMKTQLEE 703
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
343-528 3.50e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.89  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  343 EKDHLIERLYREISGLKAQLENMKTESQrvvlqlkghvseleadLAEQQHLRQQAA-DDCEFLRAEL--------DELRR 413
Cdd:pfam15619    8 ARLHKIKELQNELAELQSKLEELRKENR----------------LLKRLQKRQEKAlGKYEGTESELpqliarhnEEVRV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL-LRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS 492
Cdd:pfam15619   72 LRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELEN 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462613984  493 DQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE 528
Cdd:pfam15619  152 KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
348-599 4.11e-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: 41.09  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  348 IERLYREISGLKAQLENMKTESQRvvLQ-LKGHVSELEAdlaeqQHLRQQAADDCEflrAELDELRRQREDtekAQRSLS 426
Cdd:COG3096    787 LEELRAERDELAEQYAKASFDVQK--LQrLHQAFSQFVG-----GHLAVAFAPDPE---AELAALRQRRSE---LERELA 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  427 EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNA------EVTKQVSMARQAQVDLEREKKELEdSLERI------- 491
Cdd:COG3096    854 QHRAQEQQLRQQLDQLKEQLQLLnkLLPQANLLADETladrleELREELDAAQEAQAFIQQHGKALA-QLEPLvavlqsd 932
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  492 -------------SDQGQRKTQEQLEVLESLKQ-----------ELATSQREL-QVLQGSLE--TSAQSEANWA-----A 539
Cdd:COG3096    933 peqfeqlqadylqAKEQQRRLKQQIFALSEVVQrrphfsyedavGLLGENSDLnEKLRARLEqaEEARREAREQlrqaqA 1012
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  540 EFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSR 599
Cdd:COG3096   1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNR 1072
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
380-535 4.40e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 38.92  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  380 VSELEADLAEQQHLRQQAAddceflraeldeLRRQREDTEKAQRSLSEIERKAQANEQRYsklkekYSELvQNHADLLRK 459
Cdd:pfam07321    7 VKHLREDRAEKAVKRQEQA------------LAAARAAHQQAQASLQDYRAWRPQEEQRL------YAEI-QGKLVLLKE 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613984  460 NAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEA 535
Cdd:pfam07321   68 LEKVKQQVALLRENEADLEKQVAEARQQLEAEREalrQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELEEF 146
PRK09039 PRK09039
peptidoglycan -binding protein;
407-568 4.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  407 ELDELRRQ-----------REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqv 475
Cdd:PRK09039    54 ALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-------- 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  476 dlerekkeleDSLERISDQGQRktqeQLEVLeslKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKErdsLVSGA 555
Cdd:PRK09039   126 ----------DSEKQVSARALA----QVELL---NQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR---LNVAL 185
                          170
                   ....*....|...
gi 2462613984  556 AHREEELSALRKE 568
Cdd:PRK09039   186 AQRVQELNRYRSE 198
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
340-576 5.58e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  340 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFlraeldELRRQREDTE 419
Cdd:pfam02463  781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE------EQKLEKLAEE 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK-NAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRK 498
Cdd:pfam02463  855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKeKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  499 TQ------EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:pfam02463  935 EEpeelllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014

                   ....
gi 2462613984  573 QLKL 576
Cdd:pfam02463 1015 TCQR 1018
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
360-572 5.91e-03

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: 39.63  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  360 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE------------ 427
Cdd:pfam00261    1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEaekaadesergr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  428 --IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMarqAQVDLEREKKELEDSLERISD--QGQRKTQEQL 503
Cdd:pfam00261   81 kvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVV---VEGDLERAEERAELAESKIVEleEELKVVGNNL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  504 EVLESlkQELATSQRE------LQVLQGSLEtsaqsEANWAAEFAE-----LEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:pfam00261  158 KSLEA--SEEKASEREdkyeeqIRFLTEKLK-----EAETRAEFAErsvqkLEKEVDRLEDELEAEKEKYKAISEELDQT 230
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
406-618 8.48e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  406 AELDELRRQREDTEKAQRSLsEIERKAQANEQRYSKLKEKYselvqnhaDLLRK----NAEVTKQVSMARQAQVDLEREK 481
Cdd:pfam06160  237 KEIQQLEEQLEENLALLENL-ELDEAEEALEEIEERIDQLY--------DLLEKevdaKKYVEKNLPEIEDYLEHAEEQN 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  482 KELEDSLERIsDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE--TSAQSE-----ANWAAEFAELEKERDSLVSG 554
Cdd:pfam06160  308 KELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEekEVAYSElqeelEEILEQLEEIEEEQEEFKES 386
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  555 AAH-REEELSAlRKELQDTQLKLASTEESMCQ-----LAKDQRKMLLVGSRKaaeqvIQDALNQLEEPPL 618
Cdd:pfam06160  387 LQSlRKDELEA-REKLDEFKLELREIKRLVEKsnlpgLPESYLDYFFDVSDE-----IEDLADELNEVPL 450
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
393-521 8.93e-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: 39.99  E-value: 8.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  393 LRQQAADDCEFLRAELD-ELRRQREDTEKAQRSLSEIERKAQaneqRYSKLKEKySELVQNHADLLRKNAEVTKQVS--M 469
Cdd:pfam05262  186 LREDNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQI----DADKAQQK-ADFAQDNADKQRDEVRQKQQEAknL 260
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  470 ARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVL--------ESLKQELATSQRELQ 521
Cdd:pfam05262  261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEAlkakdhkaFDLKQESKASEKEAE 320
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
345-568 9.50e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 39.67  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  345 DHLIErlyreISGLKAQLENMKTESQRVVL-------QLKGHVSE-------LEADLAEQQHLRQQAADDCEFLRAELDE 410
Cdd:COG0497    123 ELLVD-----IHGQHEHQSLLDPDAQRELLdafagleELLEEYREayrawraLKKELEELRADEAERARELDLLRFQLEE 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  411 LRRQR----EDTEKAQrslseiERKAQAN-EQRYSKLKEKYSELVQNH---ADLLRK-----------NAEVTKQVSMAR 471
Cdd:COG0497    198 LEAAAlqpgEEEELEE------ERRRLSNaEKLREALQEALEALSGGEggaLDLLGQalralerlaeyDPSLAELAERLE 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  472 QAQVDLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQ-------ELATSQRELQVLQGSLETSAQSEANWAAEFA 542
Cdd:COG0497    272 SALIELEEAASELRRYLDSLEFDPERleEVEERLALLRRLARkygvtveELLAYAEELRAELAELENSDERLEELEAELA 351
                          250       260
                   ....*....|....*....|....*.
gi 2462613984  543 ELEKErdslVSGAAhreEELSALRKE 568
Cdd:COG0497    352 EAEAE----LLEAA---EKLSAARKK 370
PRK12704 PRK12704
phosphodiesterase; Provisional
456-615 9.92e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  456 LLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEslkQELATSQRELQVLQGSLEtsaQSEA 535
Cdd:PRK12704    23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLL---QKEE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613984  536 NwaaefaeLEKERDSLvsgaAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PRK12704    97 N-------LDRKLELL----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE 165
 
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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