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Conserved domains on  [gi|1907162016|ref|XP_036020880|]
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huntingtin-interacting protein 1 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
15-281 9.00e-93

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: 296.13  E-value: 9.00e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   15 YTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   94 NELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELN 172
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  173 LFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKD 246
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907162016  247 LFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 281
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
789-987 2.99e-91

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


:

Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 288.88  E-value: 2.99e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   789 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 868
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   869 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 947
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1907162016   948 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 987
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
463-555 3.66e-29

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: 435390 [Multi-domain]  Cd Length: 93  Bit Score: 111.65  E-value: 3.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  463 KNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWL 542
Cdd:pfam16515    1 KNAETTKQLTVTQQAQEEVERVKKQLEFEVERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGEQLS 80
                           90
                   ....*....|...
gi 1907162016  543 TQIAELEKEQGSL 555
Cdd:pfam16515   81 SQLAALQAEKERL 93
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
364-619 6.98e-13

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  364 GQLDNMKIESQRAML-------QLKGRVSELEAELAE-QQHLGRQAmDDCEFLRTELDELKRQREDTEKAQRSLTEIERK 435
Cdd:COG1196    147 EEIINAKPEERRKLIeeaagvsKYKERKEEAERKLERtEENLERLE-DLLEELEKQLEKLERQAEKAERYQELKAELREL 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  436 AQANEQ-RYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLK 514
Cdd:COG1196    226 ELALLLaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  515 HElatsRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATV---AAQREEELSALRDQLESTQIKLAGAQESMCQQV 591
Cdd:COG1196    306 LL----RERLEELENELEELEERLEELKEKIEALKEELEERETLleeLEQLLAELEEAKEELEEKLSALLEELEELFEAL 381
                          250       260
                   ....*....|....*....|....*...
gi 1907162016  592 KDQRKTLLAgIRKAAEREIQEALSQLEE 619
Cdd:COG1196    382 REELAELEA-ELAEIRNELEELKREIES 408
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
15-281 9.00e-93

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: 296.13  E-value: 9.00e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   15 YTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   94 NELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELN 172
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  173 LFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKD 246
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907162016  247 LFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 281
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
789-987 2.99e-91

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 288.88  E-value: 2.99e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   789 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 868
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   869 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 947
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1907162016   948 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 987
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
16-128 4.58e-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: 263.82  E-value: 4.58e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   16 TVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 95
Cdd:cd17013      2 TVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162016   96 LSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17013     82 LSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
I_LWEQ pfam01608
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ...
839-985 1.64e-59

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


Pssm-ID: 426343 [Multi-domain]  Cd Length: 149  Bit Score: 200.12  E-value: 1.64e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  839 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 918
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162016  919 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 985
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLVQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
15-135 1.41e-36

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 133.91  E-value: 1.41e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016    15 YTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSLRY 92
Cdd:smart00273    3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRN 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907162016    93 KNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 135
Cdd:smart00273   83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
463-555 3.66e-29

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: 435390 [Multi-domain]  Cd Length: 93  Bit Score: 111.65  E-value: 3.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  463 KNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWL 542
Cdd:pfam16515    1 KNAETTKQLTVTQQAQEEVERVKKQLEFEVERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGEQLS 80
                           90
                   ....*....|...
gi 1907162016  543 TQIAELEKEQGSL 555
Cdd:pfam16515   81 SQLAALQAEKERL 93
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
364-619 6.98e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  364 GQLDNMKIESQRAML-------QLKGRVSELEAELAE-QQHLGRQAmDDCEFLRTELDELKRQREDTEKAQRSLTEIERK 435
Cdd:COG1196    147 EEIINAKPEERRKLIeeaagvsKYKERKEEAERKLERtEENLERLE-DLLEELEKQLEKLERQAEKAERYQELKAELREL 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  436 AQANEQ-RYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLK 514
Cdd:COG1196    226 ELALLLaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  515 HElatsRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATV---AAQREEELSALRDQLESTQIKLAGAQESMCQQV 591
Cdd:COG1196    306 LL----RERLEELENELEELEERLEELKEKIEALKEELEERETLleeLEQLLAELEEAKEELEEKLSALLEELEELFEAL 381
                          250       260
                   ....*....|....*....|....*...
gi 1907162016  592 KDQRKTLLAgIRKAAEREIQEALSQLEE 619
Cdd:COG1196    382 REELAELEA-ELAEIRNELEELKREIES 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
352-619 8.92e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 8.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 429
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  430 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV 509
Cdd:TIGR02168  256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  510 ---LENLKHELATSRQELQVLHSNLE------TSAQSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:TIGR02168  329 eskLDELAEELAELEEKLEELKEELEsleaelEELEAELEELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907162016  580 LAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:TIGR02168  409 LERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEE 447
PTZ00121 PTZ00121
MAEBL; Provisional
370-619 2.95e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRsLTEIERKAQANEQRYSKLKEK 449
Cdd:PTZ00121  1458 KAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKK 1535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  450 YSELVQ----NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVL----ENLKHELATSR 521
Cdd:PTZ00121  1536 ADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKA 1615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  522 QELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAG 601
Cdd:PTZ00121  1616 EEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
                          250
                   ....*....|....*...
gi 1907162016  602 IRKAAEREIQEALSQLEE 619
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEA 1712
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
339-612 2.68e-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: 54.74  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  339 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 415
Cdd:pfam17380  280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  416 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdLEREKkeladsfarv 495
Cdd:pfam17380  351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKI-LEEER---------- 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  496 sdqaQRKTQEQQDVLENLKHELATSRQ-ELQVLHsnletsaQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:pfam17380  412 ----QRKIQQQKVEMEQIRAEQEEARQrEVRRLE-------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907162016  575 STQIKLAGAQES----MCQQVKDQRKTLL--AGIRKAAEREIQE 612
Cdd:pfam17380  481 KEKRDRKRAEEQrrkiLEKELEERKQAMIeeERKRKLLEKEMEE 524
mukB PRK04863
chromosome partition protein MukB;
386-547 8.08e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.42  E-value: 8.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  386 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 465
Cdd:PRK04863   500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  466 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENLKH------ELATSRQ 522
Cdd:PRK04863   576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsgeefedSQDVTEYMQQLLEREREltverdELAARKQ 655
                          170       180
                   ....*....|....*....|....*
gi 1907162016  523 ELQVLHSNLETSAQSEAKWLTQIAE 547
Cdd:PRK04863   656 ALDEEIERLSQPGGSEDPRLNALAE 680
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
408-566 1.56e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 41.20  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKR----QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQA--QVDL 481
Cdd:COG1579     15 LDLEKDRLEPrikeIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVKDEreLRAL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELADSFARVSDQAQRktqeqqdvLENLKHELATSRQELQVLHSNLETS-AQSEAKWLTQIAELEKEQGSLATVAA 560
Cdd:COG1579     95 NIEIQIAKERINSLEDELAE--------LMEEIEKLEKEIEDLKERLERLEKNlAEAEARLEEEVAEIREEGQELSSKRE 166

                   ....*.
gi 1907162016  561 QREEEL 566
Cdd:COG1579    167 ELKEKL 172
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
411-590 3.43e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  411 ELDELKRQREDTEKAQR-SLTEIERKA-------QANEQRYSKLKEKY-SELVQNHADLLRKNAEVTKQVSVARQAQVDL 481
Cdd:TIGR02794   51 QANRIQQQKKPAAKKEQeRQKKLEQQAeeaekqrAAEQARQKELEQRAaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELADSFARVSDQAQRKTQEqqdvlENLKHELATSRQELQVLHSNLETSAQSEA-------------KWLTQIAEL 548
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEAAKQAEE-----EAKAKAAAEAKKKAEEAKKKAEAEAKAKAeaeakakaeeakaKAEAAKAKA 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907162016  549 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQ 590
Cdd:TIGR02794  206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
443-577 3.74e-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: 40.39  E-value: 3.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   443 YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADsfarvsdQAQRKTQEQQDVLENLKHELATSRQ 522
Cdd:smart00787  160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD-------RAKEKLKKLLQEIMIKVKKLEELEE 232
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162016   523 ELQVLHSNLETSAQSEAKWLTQIAELEKeqgSLATVAAQREEELSALRDQLESTQ 577
Cdd:smart00787  233 ELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQ 284
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
344-597 6.27e-03

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 40.04  E-value: 6.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   344 NKDEKDHLIERLYREISGLTGQLDNMK--IESQRAMLQ-LKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELK 416
Cdd:smart00806   72 NVEELDEVKKHIDDEIDTLQNELDEVKqaLESQREAIQrLKERQQNSAANIARpaasPSPVLASSSSAISLANNPDKLNK 151
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   417 RQREDTEKAQRSLTEIeRKAQANEQrySKLKEKYSELVQNHADLLRKNAEVTKQVSVAR--QAQVDLEREKKELADSFAR 494
Cdd:smart00806  152 EQRAELKSLQRELAVL-RQTHNSFF--TEIKESIKDILEKIDKFKSSSLSASGSSNRAYveSSKKKLSEDSDSLLTKVDD 228
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   495 VSDQ--------AQRKTQEQQDVLENLKHELATSRQELQvlhsNLETSAQSEAKWLTQI--AELEK---EQGSLATvaaq 561
Cdd:smart00806  229 LQDIiealrkdvAQRGVRPSKKQLETVQKELETARKELK----KMEEYIDIEKPIWKKIweAELDKvceEQQFLTL---- 300
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1907162016   562 REEELSALRDQLESTQIKLAGAQESMCQQVKDQRKT 597
Cdd:smart00806  301 QEDLIADLKEDLEKAEETFDLVEQCCEEQEKGPSKN 336
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
15-281 9.00e-93

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: 296.13  E-value: 9.00e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   15 YTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:pfam07651    2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   94 NELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELN 172
Cdd:pfam07651   82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  173 LFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKD 246
Cdd:pfam07651  160 LQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907162016  247 LFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 281
Cdd:pfam07651  239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ILWEQ smart00307
I/LWEQ domain; Thought to possess an F-actin binding function.
789-987 2.99e-91

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


Pssm-ID: 214607 [Multi-domain]  Cd Length: 200  Bit Score: 288.88  E-value: 2.99e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   789 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 868
Cdd:smart00307    1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   869 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 947
Cdd:smart00307   81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1907162016   948 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 987
Cdd:smart00307  161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
16-128 4.58e-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: 263.82  E-value: 4.58e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   16 TVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 95
Cdd:cd17013      2 TVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162016   96 LSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17013     82 LSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
16-128 5.52e-68

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: 222.54  E-value: 5.52e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   16 TVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 95
Cdd:cd17006      2 AISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSR 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162016   96 LSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
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 ...
839-985 1.64e-59

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


Pssm-ID: 426343 [Multi-domain]  Cd Length: 149  Bit Score: 200.12  E-value: 1.64e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  839 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 918
Cdd:pfam01608    1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162016  919 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 985
Cdd:pfam01608   81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLVQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
17-128 3.96e-55

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: 186.61  E-value: 3.96e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 96
Cdd:cd17014      3 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNI 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907162016   97 SDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17014     83 RETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
16-128 5.54e-41

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: 146.37  E-value: 5.54e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   16 TVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR- 91
Cdd:cd16986      2 EKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDa 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907162016   92 YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd16986     81 WLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
15-135 1.41e-36

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 133.91  E-value: 1.41e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016    15 YTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSLRY 92
Cdd:smart00273    3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRN 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907162016    93 KNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 135
Cdd:smart00273   83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
463-555 3.66e-29

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: 435390 [Multi-domain]  Cd Length: 93  Bit Score: 111.65  E-value: 3.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  463 KNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWL 542
Cdd:pfam16515    1 KNAETTKQLTVTQQAQEEVERVKKQLEFEVERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGEQLS 80
                           90
                   ....*....|...
gi 1907162016  543 TQIAELEKEQGSL 555
Cdd:pfam16515   81 SQLAALQAEKERL 93
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
17-128 5.66e-25

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: 100.46  E-value: 5.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 96
Cdd:cd17007      3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907162016   97 SDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17007     83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
364-619 6.98e-13

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  364 GQLDNMKIESQRAML-------QLKGRVSELEAELAE-QQHLGRQAmDDCEFLRTELDELKRQREDTEKAQRSLTEIERK 435
Cdd:COG1196    147 EEIINAKPEERRKLIeeaagvsKYKERKEEAERKLERtEENLERLE-DLLEELEKQLEKLERQAEKAERYQELKAELREL 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  436 AQANEQ-RYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLK 514
Cdd:COG1196    226 ELALLLaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  515 HElatsRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATV---AAQREEELSALRDQLESTQIKLAGAQESMCQQV 591
Cdd:COG1196    306 LL----RERLEELENELEELEERLEELKEKIEALKEELEERETLleeLEQLLAELEEAKEELEEKLSALLEELEELFEAL 381
                          250       260
                   ....*....|....*....|....*...
gi 1907162016  592 KDQRKTLLAgIRKAAEREIQEALSQLEE 619
Cdd:COG1196    382 REELAELEA-ELAEIRNELEELKREIES 408
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
346-619 1.23e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 72.44  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNMK---IESQRAMLQLKGRVSELEAELAEQQHLGRQamddcefLRTELDELKRQREDT 422
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQeelEEAEKEIEELKSELEELREELEELQEELLE-------LKEEIEELEGEISLL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  423 -EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQR 501
Cdd:COG1196    308 rERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAE 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  502 KTQEQqdvlENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 581
Cdd:COG1196    388 LEAEL----AEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLK 463
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907162016  582 GAQESMCQQVKDQRKtllagirkaAEREIQEALSQLEE 619
Cdd:COG1196    464 ELERELAELQEELQR---------LEKELSSLEARLDR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
352-619 8.92e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 8.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 429
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  430 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV 509
Cdd:TIGR02168  256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  510 ---LENLKHELATSRQELQVLHSNLE------TSAQSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:TIGR02168  329 eskLDELAEELAELEEKLEELKEELEsleaelEELEAELEELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907162016  580 LAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:TIGR02168  409 LERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEE 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
372-619 9.88e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 9.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  372 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK-AQRSLTEIERKAQANEQRYSKLKEKY 450
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  451 SELVQNHADL--LRKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQR---KTQEQQDVLENLKHELATSRQEL 524
Cdd:TIGR02168  761 AEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  525 QVLHSNLETSAQseakwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRK 604
Cdd:TIGR02168  841 EDLEEQIEELSE-------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE--LESKRS 911
                          250
                   ....*....|....*
gi 1907162016  605 AAEREIQEALSQLEE 619
Cdd:TIGR02168  912 ELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
346-580 4.01e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.43  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNMKIESQRAML---QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDT 422
Cdd:COG1196    698 RSLEDLLEELRRQLEELERQLEELKRELAALEEeleQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  423 EKAQRSLT-----------EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADS 491
Cdd:COG1196    778 KEEIEELEekrqalqeeleELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  492 FARVSDQ---AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSA 568
Cdd:COG1196    858 LEELKEEleeLEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEE 937
                          250
                   ....*....|..
gi 1907162016  569 LRDQLESTQIKL 580
Cdd:COG1196    938 EYEDTLETELER 949
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
352-620 4.59e-11

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.05  E-value: 4.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLDnmKIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK----AQR 427
Cdd:COG1196    669 LKELEEELAELEAQLE--KLEEELK--SLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSrleeLEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  428 SLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQ 507
Cdd:COG1196    745 ELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  508 DV---LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQ 584
Cdd:COG1196    825 RLeqeIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEEL-------EDELKELEEEKEELEEELRELE 897
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907162016  585 ESMCQ-----QVKDQRKTLLAGIRKAAEREIQEALSQLEEP 620
Cdd:COG1196    898 SELAElkeeiEKLRERLEELEAKLERLEVELPELEEELEEE 938
PTZ00121 PTZ00121
MAEBL; Provisional
370-619 2.95e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRsLTEIERKAQANEQRYSKLKEK 449
Cdd:PTZ00121  1458 KAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKK 1535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  450 YSELVQ----NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVL----ENLKHELATSR 521
Cdd:PTZ00121  1536 ADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKA 1615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  522 QELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAG 601
Cdd:PTZ00121  1616 EEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
                          250
                   ....*....|....*...
gi 1907162016  602 IRKAAEREIQEALSQLEE 619
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEA 1712
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
345-617 5.92e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.08  E-value: 5.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  345 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 421
Cdd:TIGR02169  204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  422 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvaRQAQVDLE 482
Cdd:TIGR02169  284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---DKLTEEYA 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  483 REKKELADSFARV------SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLA 556
Cdd:TIGR02169  361 ELKEELEDLRAELeevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  557 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 617
Cdd:TIGR02169  441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
17-126 1.09e-08

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: 54.20  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:cd03564      3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907162016   94 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 126
Cdd:cd03564     83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
347-619 2.55e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 58.23  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  347 EKDHLIERLYReisglTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQhlgRQAMDDCEFLRTELDELKRQREDTEKAQ 426
Cdd:COG0419    155 ERKEILDELFG-----LEKYEKLSELLKEVIKEAKAKIEELEGQLSELL---EDIEDLLEALEEELKELKKLEEIQEEQE 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  427 RSltEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdqaQRKTQEq 506
Cdd:COG0419    227 EE--ELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEEL-----------EEKIER- 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  507 qdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQES 586
Cdd:COG0419    293 ---LEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEK-LESELEELAEEKNELAKLLEERLKELEE 368
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907162016  587 MCQQVKDQRKTLLAgIRKAAEREIQEALSQLEE 619
Cdd:COG0419    369 RLEELEKELEKALE-RLKQLEEAIQELKEELAE 400
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
358-617 3.54e-08

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 57.34  E-value: 3.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  358 EISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGrqamDDCEFLRTELDELKRQREdteKAQRSLTEIERKAQ 437
Cdd:COG4372     75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKAR----QEREAVRQELAAARQNLA---KAQQELARLTKQAQ 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  438 ANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarqaQVDLERekKELADSFARVSDQAQrKTQEQQDVLENLKHEL 517
Cdd:COG4372    148 DLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASAT-----QLKSQV--LDLKLRSAQIEQEAQ-NLATRANAAQARTEEL 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  518 ATSRQELQVLHSNLETSAqseakwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ-------ESMCQQ 590
Cdd:COG4372    220 ARRAAAAQQTAQAIQQRD-------AQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEayyqayvRLRQQA 292
                          250       260
                   ....*....|....*....|....*....
gi 1907162016  591 VKDQRKTLLAG--IRKAAEREIQEALSQL 617
Cdd:COG4372    293 AATQRGQVLAGaaQRVAQAQAQAQAQAQL 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
350-581 1.83e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  350 HLIERLYREISGLTGQldnmkIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELK-----------R 417
Cdd:TIGR02168  747 ERIAQLSKELTELEAE-----IEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaaN 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  418 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD 497
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  498 QAQ---RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwltQIAELEK-EQGSLATVAAQREEELSALRDQL 573
Cdd:TIGR02168  902 ELReleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-------RLSEEYSlTLEEAEALENKIEDDEEEARRRL 974

                   ....*...
gi 1907162016  574 ESTQIKLA 581
Cdd:TIGR02168  975 KRLENKIK 982
46 PHA02562
endonuclease subunit; Provisional
337-582 2.39e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 54.64  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  337 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 407
Cdd:PHA02562   165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 484
Cdd:PHA02562   239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  485 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 564
Cdd:PHA02562   308 LKELQHSL--------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
                          250
                   ....*....|....*...
gi 1907162016  565 ELSALRDQLESTQIKLAG 582
Cdd:PHA02562   380 ELAKLQDELDKIVKTKSE 397
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
339-612 2.68e-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: 54.74  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  339 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 415
Cdd:pfam17380  280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  416 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdLEREKkeladsfarv 495
Cdd:pfam17380  351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKI-LEEER---------- 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  496 sdqaQRKTQEQQDVLENLKHELATSRQ-ELQVLHsnletsaQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:pfam17380  412 ----QRKIQQQKVEMEQIRAEQEEARQrEVRRLE-------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907162016  575 STQIKLAGAQES----MCQQVKDQRKTLL--AGIRKAAEREIQE 612
Cdd:pfam17380  481 KEKRDRKRAEEQrrkiLEKELEERKQAMIeeERKRKLLEKEMEE 524
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
345-602 3.66e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  345 KDEKDHLIERLYREISGLTGQLD---------NMKIES-QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDE 414
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEelrlevselEEEIEElQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  415 LKRQREDTEKA------------------QRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR- 475
Cdd:TIGR02168  328 LESKLDELAEElaeleekleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEa 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  476 ---QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAELEKEq 552
Cdd:TIGR02168  408 rleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE---EALEELREELEEAEQALDAAERE- 483
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907162016  553 gslatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGI 602
Cdd:TIGR02168  484 ----------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSG--LSGI 521
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
418-619 4.61e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 53.95  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  418 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD 497
Cdd:COG1196    665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  498 QAQRKTQEQ---QDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:COG1196    745 ELEELEEELeelQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRE 824
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907162016  575 STQIKLAGAQESMcQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 619
Cdd:COG1196    825 RLEQEIEELEEEI-EELEEKLDELEEEL-EELEKELEELKEELEE 867
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
379-619 4.61e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 458
Cdd:PRK03918   190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  459 DLLRKNAEVTKQVSvarqaqvDLErEKKELADSFARVSdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQ 536
Cdd:PRK03918   270 ELKKEIEELEEKVK-------ELK-ELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  537 SEAKWLT-QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALS 615
Cdd:PRK03918   338 ERLEELKkKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEIS 408

                   ....
gi 1907162016  616 QLEE 619
Cdd:PRK03918   409 KITA 412
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
375-606 5.09e-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: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 53.35  E-value: 5.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  375 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 450
Cdd:pfam07888   28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  451 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSN 530
Cdd:pfam07888   97 EELEEKYKELSRSGEELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEE-EAERKQ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  531 LETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRK 604
Cdd:pfam07888  176 LQAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERK 252

                   ..
gi 1907162016  605 AA 606
Cdd:pfam07888  253 VE 254
mukB PRK04863
chromosome partition protein MukB;
386-547 8.08e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.42  E-value: 8.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  386 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 465
Cdd:PRK04863   500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  466 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENLKH------ELATSRQ 522
Cdd:PRK04863   576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsgeefedSQDVTEYMQQLLEREREltverdELAARKQ 655
                          170       180
                   ....*....|....*....|....*
gi 1907162016  523 ELQVLHSNLETSAQSEAKWLTQIAE 547
Cdd:PRK04863   656 ALDEEIERLSQPGGSEDPRLNALAE 680
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
346-604 8.62e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 8.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNMKIEsqraMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKA 425
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  426 QRSLTEI------------ERKAQANEQRYSKLKEKYSelVQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSF 492
Cdd:TIGR02168  847 IEELSEDieslaaeieeleELIEELESELEALLNERAS--LEEALALLRSELEeLSEELRELESKRSELRRELEELREKL 924
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  493 ARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETsaqSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 572
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED---DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907162016  573 LE--STQIKlagaqesmcqQVKDQRKTLLAGIRK 604
Cdd:TIGR02168 1002 YDflTAQKE----------DLTEAKETLEEAIEE 1025
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
344-564 9.45e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 52.84  E-value: 9.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  344 NKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLgRQAMDDCEFLRTELDELKRQREdt 422
Cdd:COG0419    527 LKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRqLEDRLQELKELLEELRLL-RTRKEELEELRERLKELKKKLK-- 603
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  423 eKAQRSLTEIERKAQANE--QRYSKLKEKYSELvqnhADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQ 500
Cdd:COG0419    604 -ELEERLSQLEELLQSLElsEAENELEEAEEEL----ESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIE 678
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162016  501 RKTQ--EQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 564
Cdd:COG0419    679 NEEQleEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALEL 744
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
352-619 1.27e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 431
Cdd:PRK02224   178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  432 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQRKTQEQQD 508
Cdd:PRK02224   239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARRE 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  509 VLEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQ 577
Cdd:PRK02224   318 ELEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162016  578 IKLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 619
Cdd:PRK02224   398 ERFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
PTZ00121 PTZ00121
MAEBL; Provisional
370-619 1.89e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 448
Cdd:PTZ00121  1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  449 KYSElvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKElADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLH 528
Cdd:PTZ00121  1465 KAEE--AKKADEAKKKAEEAKK---ADEAKKKAEEAKKK-ADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  529 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAA 606
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKAE 1616
                          250
                   ....*....|....
gi 1907162016  607 EREIQ-EALSQLEE 619
Cdd:PTZ00121  1617 EAKIKaEELKKAEE 1630
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
346-619 2.24e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNMkiESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 401
Cdd:PRK02224   387 EELEEEIEELRERFGDAPVDLGNA--EDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  402 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 472
Cdd:PRK02224   465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  473 VARQAQVDLEREKKELADSFARVSDQAQrKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAkwltQIAELEKEQ 552
Cdd:PRK02224   541 ELRERAAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAELKERIESLERIRTLLAAIADAED----EIERLREKR 615
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162016  553 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 619
Cdd:PRK02224   616 EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
413-619 2.35e-06

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 51.26  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  413 DELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF 492
Cdd:COG4942     38 KQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRRL 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  493 ARVSDQAQRKTQEQQDVLENLKHElATSRQELQVLHSNLetsAQSEAKwltQIAELEKEQGSLATVAAQREEElsalRDQ 572
Cdd:COG4942    118 AEQLAALQRSGRNPPPALLVSPED-AQRSVRLAIYYGAL---NPARAE---RIDALKATLKQLAAVRAEIAAE----QAE 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907162016  573 LESTQIKLAGAQESMCQQVKDQRKTLlagirKAAEREIQEALSQLEE 619
Cdd:COG4942    187 LTTLLSEQRAQQAKLAQLLEERKKTL-----AQLNSELSADQKKLEE 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
352-570 3.32e-06

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 50.49  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLdnmkIESQRAMLQLKGRVSELEAELA--EQQHLGRQamddcEFLRTELDELKRQREDTekaqrSL 429
Cdd:COG4942     68 LKSLETEIASLEAQL----IETADDLKKLRKQIADLNARLNalEVQEREQR-----RRLAEQLAALQRSGRNP-----PP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  430 TEIERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAqvdLEREKKELADSFARVSDQAQR---KTQEQ 506
Cdd:COG4942    134 ALLVSPEDA--QRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAE---IAAEQAELTTLLSEQRAQQAKlaqLLEER 208
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162016  507 QDVLENLKHELATSRQELQVLHSNletsaqseakwltqIAELEKEQGSLATVAAQREEELSALR 570
Cdd:COG4942    209 KKTLAQLNSELSADQKKLEELRAN--------------ESRLKNEIASAEAAAAKAREAAAAAE 258
Filament pfam00038
Intermediate filament protein;
356-574 6.01e-06

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 49.14  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  356 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 432
Cdd:pfam00038   53 EREIRELRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRQSAEADIVGLRKDLDEATLARVDLEMKIESLKE- 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  433 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSFARVSD 497
Cdd:pfam00038  132 -------ELAF--LKKNHEEEV---RELQSQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaEKNREEAEEWYQSKLE 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  498 QAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 572
Cdd:pfam00038  200 ELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQQIRQE 278

                   ..
gi 1907162016  573 LE 574
Cdd:pfam00038  279 MA 280
PTZ00121 PTZ00121
MAEBL; Provisional
370-619 6.08e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 6.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTE----LDELKRQREDTEKAQRSLTEIERKA-----QANE 440
Cdd:PTZ00121  1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEaeaaADEAEAAEEKAEAAEKKKEEAKKKAdaakkKAEE 1389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  441 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSfARVSDQAQRKTQEQQDVlENLKHELA 518
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEE-AKKADEAKKKAEEAKKA-EEAKKKAE 1467
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  519 TSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTL 598
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
                          250       260
                   ....*....|....*....|.
gi 1907162016  599 LAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEE 1568
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
370-619 6.23e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 50.54  E-value: 6.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 449
Cdd:pfam01576  259 KNAALKKLRELEAQLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  450 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVlENLKHELATSR 521
Cdd:pfam01576  336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAKQDS-EHKRKKLEGQL 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  522 QELQVLHSNLETSAQSEAKWLTQI-AELEKEQGSLATVAAQR---EEELSALRDQL--------ESTQIKLAGAqeSMCQ 589
Cdd:pfam01576  415 QELQSRLSESERQRAELAEKLSKLqSELESVSSLLNEAEGKNiklSKDVSSLESQLqdtqellqEETRQKLNLS--SRLR 492
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907162016  590 QVKDQRKTLLAGI------RKAAEREIQEALSQLEE 619
Cdd:pfam01576  493 QLEDEKNSLQEQLeeeeeaKRNVERQLQTLQAQLSD 528
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
362-595 7.28e-06

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227608 [Multi-domain]  Cd Length: 1213  Bit Score: 50.31  E-value: 7.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  362 LTGQLDNMKIESQRAMLQLKGRVSELEAE---LAEQQHLGRQAM-DDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQ 437
Cdd:COG5283      9 GATAIDNNDTIAVKNINVLKSSIKDSTQFwkmLEKQQKLTKDGLsASKGKYEGLSEAMEKQKKAYEDLKQEVKEVNRATQ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  438 ANEQRYSKLKEKYSelvqnHADLLRKNAevTKQVSVARQAQVDLEREKKELADSFArvsdQAQRKTQEQQDVLENLKHEL 517
Cdd:COG5283     89 ASKKAYQEYNAQYT-----QAENKLRSL--SGQFGVASEQLMLQQKEIQRLQYAIS----TLNKSMAAQARLLEQTGNKF 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162016  518 ATSRQELqvlhSNLETSAQSEAKWLTqiaelekEQGSLATVAAqreeelSALRDQLESTQIKLAGAQESMCQQVKDQR 595
Cdd:COG5283    158 GTADAKV----VGLRESFGRQTEALN-------KQLERTKKVA------DALTYVLDEAQQKLSQALSARLERLQESR 218
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
338-619 1.07e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.25  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  338 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 407
Cdd:TIGR04523  376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 483
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  484 EKKELADSFarvsDQAQRKTQEQQDVL--ENLKHELATSRQELQVLHSNLE--TSAQSEAKWL-----TQIAELEKEQGS 554
Cdd:TIGR04523  532 EKKEKESKI----SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKslKKKQEEKQELidqkeKEKKDLIKEIEE 607
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  555 LATVAAQREEELSALRDQ---LESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 619
Cdd:TIGR04523  608 KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEiiKKIKESKTKIDD 677
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
407-619 1.45e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  407 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 475
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  476 QAQVDLEREKKELADSFARVSDQaQRKTQEQQDVLENLKHELATSR-QELQVLHSNLETSAQseaKWLTQIAELEKEQGS 554
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEEL-EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVS---RIEARLREIEQKLNR 823
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162016  555 LATVAAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 619
Cdd:TIGR02169  824 LTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL-EEELEELEAALRDLES 882
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
429-619 1.48e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 49.00  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  429 LTEIERKAQAneqrYSKLKEKYSELVQNHADLLRKNaEVTKQvsvarqaqvDLEREKKELADSFARVSDQaqrkTQEQQD 508
Cdd:pfam01576  168 LAEEEEKSKS----LNKLKNKHEAMISDLEDRLKKE-EKGRQ---------ELEKAKRKLEGESSDLQEQ----IAELQA 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  509 VLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-----------LEKEQGSLATVAAQR---EEELSALRDQLE 574
Cdd:pfam01576  230 QIAELRAQLAKKEEELQAALARLEEETAQKNAALKKLREleaqlselqedLESERAARAKAEKQRrdlGEELEALKTELE 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907162016  575 STQIKLAGAQEsmcqqVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:pfam01576  310 DTLDTTAAQQE-----LRSKREQEVTELKKALEEETRSHEAQLQE 349
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
374-619 1.60e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  374 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 453
Cdd:TIGR00618  527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  454 VQNHADLLRKNAEVTKQVSVARQAQvdleREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSNLET 533
Cdd:TIGR00618  593 TVRLQDLTEKLSEAEDMLACEQHAL----LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSI 667
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  534 SAQSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREI 610
Cdd:TIGR00618  668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSL 745

                   ....*....
gi 1907162016  611 QEALSQLEE 619
Cdd:TIGR00618  746 KELMHQART 754
PTZ00121 PTZ00121
MAEBL; Provisional
370-619 2.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  370 KIESQRAMLQLKGRvselEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSlteieRKAQANEQRYSKLKEK 449
Cdd:PTZ00121  1571 KAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKK 1641
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  450 YSELVQNhADLLRKnAEVTKQVSVARQAQVDLEREKKeladsfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHS 529
Cdd:PTZ00121  1642 EAEEKKK-AEELKK-AEEENKIKAAEEAKKAEEDKKK---------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  530 NLETSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAERE 609
Cdd:PTZ00121  1711 EAEEKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
                          250
                   ....*....|
gi 1907162016  610 IQEALSQLEE 619
Cdd:PTZ00121  1781 IEEELDEEDE 1790
PTZ00121 PTZ00121
MAEBL; Provisional
367-619 2.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  367 DNMKIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRtELDELKRQREDTEKAQRSLTEIER-------KAQAN 439
Cdd:PTZ00121  1403 DKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEakkadeaKKKAE 1480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  440 EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQ-----------RKTQEQQD 508
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKkaeekkkadelKKAEELKK 1559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  509 VLENLKHELATSRQELQVLHS-NLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESM 587
Cdd:PTZ00121  1560 AEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907162016  588 CQQVKDQRKTllAGIRKAAE----REIQEALSQLEE 619
Cdd:PTZ00121  1640 KKEAEEKKKA--EELKKAEEenkiKAAEEAKKAEED 1673
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
348-618 2.75e-05

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 48.17  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  348 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 414
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  415 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 472
Cdd:pfam15921  563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  473 VARQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAEL 548
Cdd:pfam15921  643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSM 718
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  549 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAA 606
Cdd:pfam15921  719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQ 798
                          330
                   ....*....|..
gi 1907162016  607 EREIQEALSQLE 618
Cdd:pfam15921  799 ERRLKEKVANME 810
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
373-618 4.28e-05

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 47.71  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  373 SQRAMLQLKGRVSELEAELAEQQH----LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKE 448
Cdd:COG5281    284 AQLEQIAALQRAGDTAAAAAAAAEaaaaMDDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGREDKQAALLAAKLAA 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  449 KYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD-QAQRKTQEQQDVLENLKHEL----ATSRQE 523
Cdd:COG5281    364 EKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAANQEGALNAREDEaEVLSTQEERRDILKNLLADAekrtARQEEL 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  524 LQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE-----LSALRDQLEsTQIKLAGAQESMCQQVKDQRKTL 598
Cdd:COG5281    444 NKALAKAKILQADKAAKAYQEDILQREAQSRGKTAAAERSQEqmtaaLKALLAFQQ-QIADLSGAKEKASDQKSLLWKAE 522
                          250       260
                   ....*....|....*....|
gi 1907162016  599 LAGIRKAAEREIQEALSQLE 618
Cdd:COG5281    523 EQYALLKEEAKQRQLQEQKA 542
PRK12705 PRK12705
hypothetical protein; Provisional
383-545 4.41e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.40  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  383 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 462
Cdd:PRK12705    37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  463 KNAEvtkqvsvarqaqvdLEREKKELADSFARVSDQAQRktQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWL 542
Cdd:PRK12705   117 RELE--------------LEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERK 177

                   ...
gi 1907162016  543 TQI 545
Cdd:PRK12705   178 AQN 180
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
346-614 6.42e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 390
Cdd:pfam10174  362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  391 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 454
Cdd:pfam10174  442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  455 QNHADLLRKNAEVTKQVSVARQAQ--VDLEREKKELADSFARVSDQAQRKTQE----QQDV---------LENLKH---- 515
Cdd:pfam10174  521 SLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerllgilreVENEKNdkdk 600
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  516 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 582
Cdd:pfam10174  601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1907162016  583 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 614
Cdd:pfam10174  681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
344-619 8.21e-05

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


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 46.63  E-value: 8.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  344 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 409
Cdd:pfam15921  265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  410 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSklKEKYSELVQNHADLLRK-NAEVTKqvsvaRQAQVDLEREK-K 486
Cdd:pfam15921  331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTE--RDQFSQESGNLDDQLQKlLADLHK-----REKELSLEKEQnK 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  487 ELADsfarvSDQAQRKTqeqqdvLENLKHELATSRQELQVLHSNLET-SAQSEAKWLTQIAELEKEQGSLatvaaqreEE 565
Cdd:pfam15921  402 RLWD-----RDTGNSIT------IDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL--------EK 462
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162016  566 LSALRDQLESTQIKLagaqESMCQQVKDQRKTLlagirKAAEREIQEALSQLEE 619
Cdd:pfam15921  463 VSSLTAQLESTKEML----RKVVEELTAKKMTL-----ESSERTVSDLTASLQE 507
mukB PRK04863
chromosome partition protein MukB;
355-592 9.47e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 9.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  355 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 428
Cdd:PRK04863   849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  429 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 477
Cdd:PRK04863   918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  478 QVDLEREKKELADSFARVSDQAQRKTQEQQ--DVLENLKHELATSRQELQV-LHSNLETSAQSEAKWL--------TQIA 546
Cdd:PRK04863   998 EQERTRAREQLRQAQAQLAQYNQVLASLKSsyDAKRQMLQELKQELQDLGVpADSGAEERARARRDELharlsanrSRRN 1077
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907162016  547 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 592
Cdd:PRK04863  1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
362-574 9.56e-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: 46.37  E-value: 9.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  362 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 433
Cdd:pfam12128  658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  434 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFARVS---------DQAQRKT 503
Cdd:pfam12128  733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQET 804
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  504 QEQQDvlENLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:pfam12128  805 WLQRR--PRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
351-619 1.17e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  351 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 429
Cdd:PRK03918   315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  430 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFARVSDQAQR 501
Cdd:PRK03918   387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEK 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  502 KTQEQQDVLENLKHELATSRQELqvlhsNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLA 581
Cdd:PRK03918   467 ELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLK 538
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907162016  582 GAQESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PRK03918   539 GEIKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
343-533 1.81e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  343 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 417
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  418 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtKQVSVARQAQVDLEREKKELADSFA 493
Cdd:TIGR02169  890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIR 968
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907162016  494 RVSDQAQRKTQEQQDVLENL-----KHE-LATSRQELQVLHSNLET 533
Cdd:TIGR02169  969 ALEPVNMLAIQEYEEVLKRLdelkeKRAkLEEERKAILERIEEYEK 1014
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
379-551 2.92e-04

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: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 44.72  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL-DELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNH 457
Cdd:pfam05557    6 ESKARLSQLQNEKKQMELEHKRARIELERKASALaRQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKNL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  458 ADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKhELATSRQELQVLHSNLETSAQS 537
Cdd:pfam05557   86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRQELELSSTNSELEELQERLD-LQKAKAQEAEQLRQNLEAQQSS 164
                          170
                   ....*....|....
gi 1907162016  538 EAKWLTQIAELEKE 551
Cdd:pfam05557  165 LAEAEQRIKELEFE 178
PTZ00121 PTZ00121
MAEBL; Provisional
369-585 3.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  369 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 445
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  446 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKELADsfARVSDQ-----AQRKTQEQQDVLENLKHE 516
Cdd:PTZ00121  1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEE--AKKDEEekkkiAHLKKEEEKKAEEIRKEK 1777
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  517 LATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAT--VAAQREEELSALRDQLESTQIKLAGAQE 585
Cdd:PTZ00121  1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADA 1848
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
344-602 3.17e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.71  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  344 NKDEKDHLIERLYREISGLTGQLDNMkiesQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDT- 422
Cdd:COG1196    787 KRQALQEELEELEEELEEAERRLDAL----ERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELk 862
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  423 ---EKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQA 499
Cdd:COG1196    863 eelEELEAEKEELEDELKELEEEKEELEEELREL---ESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEY 939
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  500 QrktQEQQDVLENLKHELATSRQELQVLhsNLETsaqseakwLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:COG1196    940 E---DTLETELEREIERLEEEIEALGPV--NLRA--------IEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKE 1006
                          250       260
                   ....*....|....*....|...
gi 1907162016  580 LAGAQESMCQQVKDQRKTLLAGI 602
Cdd:COG1196   1007 KRERFKETFDKINENFSEIFKEL 1029
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
371-580 3.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  371 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIER---KAQANEQRYSKL 446
Cdd:PRK02224   532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllaAIADAEDEIERL 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  447 KEKYSELvqnhadllrknAEVTKQvsvaRQAQVDLERE-KKELADSF--ARVsDQAQRKTQEQQDVLENLKHELATSRQE 523
Cdd:PRK02224   612 REKREAL-----------AELNDE----RRERLAEKRErKRELEAEFdeARI-EEAREDKERAEEYLEQVEEKLDELREE 675
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  524 lqvlhsnlETSAQSEAKWLT-QIAELEKEQGSLATVAAqREEELSALRD---QLESTQIKL 580
Cdd:PRK02224   676 --------RDDLQAEIGAVEnELEELEELRERREALEN-RVEALEALYDeaeELESMYGDL 727
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
408-618 3.32e-04

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 44.36  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQRSLTEI---------ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ---VSVAR 475
Cdd:COG3206    153 GRSRVIELSYTSNDPKLAAKLANALaqayladqlEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDFRAQhglTDAAR 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  476 QAQVDlEREKKELADSFARvsdqAQRKTQEQQDVLENLKHELATSRQELQVLhSNLETSAQSEAKwlTQIAELEKEQGSL 555
Cdd:COG3206    233 GQLLS-EQQLSALNTQLQS----ARARLAQAEARLASLLQLLPLGREAAALR-EVLESPTIQDLR--QQYAQVRQQIADL 304
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162016  556 ATVAAQREEELSALRDQLESTQIKLagAQESmcQQVKDQRKTLLAGIRK---AAEREIQEALSQLE 618
Cdd:COG3206    305 STELGAKHPQLVALEAQLAELRQQI--AAEL--RQILASLPNELALLEQqeaALEKELAQLKGRLS 366
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
379-618 3.36e-04

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


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 44.77  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQA---------NEQRYS----- 444
Cdd:pfam01576  746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIEAANKGRDEAVKQLKKLQAqmkdlqrelDEARASrdeif 825
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  445 --------KLKEKYSELVQNHADLlrknaevtkqvSVARQAQVDLEREKKELADsfaRVSDQAQRKTQeQQDVLENLKHE 516
Cdd:pfam01576  826 aqskesekKLKSLEAELLQLQEDL-----------AAAERARRQAQQERDELAE---EIASGNSGKSA-LLDEKRRLEAR 890
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  517 LATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEElsalRDQLESTQIKLAGAQESMCQQVKDQRK 596
Cdd:pfam01576  891 IAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESA----RQQLERQNKELKAKLQEMEGTVKSKYK 966
                          250       260
                   ....*....|....*....|..
gi 1907162016  597 TLLAgirkAAEREIQEALSQLE 618
Cdd:pfam01576  967 SSIA----ALEAKIAQLEEQLE 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
352-559 3.56e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 426
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  427 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdqaqRKTQE 505
Cdd:TIGR02169  409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------------YDLKE 476
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162016  506 QQDVLENlkhELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 559
Cdd:TIGR02169  477 EYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
345-514 4.46e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.32  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  345 KDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDtek 424
Cdd:COG1196    346 LEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLED--- 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  425 AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKtQ 504
Cdd:COG1196    423 LKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRAS-Q 501
                          170
                   ....*....|
gi 1907162016  505 EQQDVLENLK 514
Cdd:COG1196    502 GVRAVLEALE 511
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
408-533 5.17e-04

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


Pssm-ID: 429739 [Multi-domain]  Cd Length: 127  Bit Score: 41.07  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREkke 487
Cdd:pfam07926    4 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE--- 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907162016  488 lADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQ----VLHSNLET 533
Cdd:pfam07926   78 -AESAKAELEESEESWEEQKKRLEKELSELEKRIEDLNeqnkLLHDQLES 126
PTZ00121 PTZ00121
MAEBL; Provisional
414-619 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  414 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFA 493
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAE 1363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  494 RVSDQAQRKTQEQQDVLENLKHELATSRQElqvlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQL 573
Cdd:PTZ00121  1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907162016  574 ESTQIKLAgaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121  1439 KAEEAKKA---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
PTZ00121 PTZ00121
MAEBL; Provisional
414-619 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  414 ELKRQREDTEKAQRSLTEIERKA----QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAqvdlEREKKELA 489
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVE 1636
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  490 DSFARVSDQAQRKTQEQQDVLENL--KHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELS 567
Cdd:PTZ00121  1637 QLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162016  568 ALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121  1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
400-619 1.25e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  400 QAMDDCEFLRTELDELKRQREDTEKAQRslteiERKAQANEQRYSKLKEKYSELVQNHADLlrKNAEVTKQVSVARQAQV 479
Cdd:pfam17380  263 QTMTENEFLNQLLHIVQHQKAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKL--EEAEKARQAEMDRQAAI 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  480 DLEREKKELadsfarvsdqaQRKTQEQQDVLENLKHELATSRQElqvlhsnletsaqSEAKWLTQIAELEKEQgslatva 559
Cdd:pfam17380  336 YAEQERMAM-----------ERERELERIRQEERKRELERIRQE-------------EIAMEISRMRELERLQ------- 384
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  560 AQREEELSALRDQLEST-QIKLagaQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:pfam17380  385 MERQQKNERVRQELEAArKVKI---LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
408-566 1.56e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 41.20  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKR----QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQA--QVDL 481
Cdd:COG1579     15 LDLEKDRLEPrikeIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVKDEreLRAL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELADSFARVSDQAQRktqeqqdvLENLKHELATSRQELQVLHSNLETS-AQSEAKWLTQIAELEKEQGSLATVAA 560
Cdd:COG1579     95 NIEIQIAKERINSLEDELAE--------LMEEIEKLEKEIEDLKERLERLEKNlAEAEARLEEEVAEIREEGQELSSKRE 166

                   ....*.
gi 1907162016  561 QREEEL 566
Cdd:COG1579    167 ELKEKL 172
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
383-616 1.67e-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: 42.27  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  383 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 462
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  463 KNAEVTKQVSVARQ---AQVDLEREKKELADSFARVsDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 539
Cdd:pfam02463  251 EEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEE-ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162016  540 KWLTQ--IAELEKEqgsLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 616
Cdd:pfam02463  330 LKKEKeeIEELEKE---LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
HlyD pfam00529
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ...
379-579 2.00e-03

HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 41.64  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLgrqamddceflrteldelkrqredtekaqrslteiERKAQANEQRYSKLKEKYSELVQNHA 458
Cdd:pfam00529   55 DYQAALDSAEAQLAKAQAQ-----------------------------------VARLQAELDRLQALESELAISRQDYD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  459 DLLRKNAEVTKQVSVArQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQse 538
Cdd:pfam00529  100 GATAQLRAAQAAVKAA-QAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-- 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907162016  539 akwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:pfam00529  177 ----ENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
408-622 2.01e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.05  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQRSLTEIERKaqanEQRYSKLKEKYSELVQNHADLLRKNAEVTKqvsvarqaqvDLEREKKE 487
Cdd:COG0419    479 YELELEELEEELSREKEEAELREEIEEL----EKELRELEEELIELLELEEALKEELEEKLE----------KLENLLEE 544
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  488 LADSFARV-SDQAQRKTQEQQDVLENLKHELATSRQEL---QVLHSNLETSAQSEAKW------LTQIAELEKEQGSLAT 557
Cdd:COG0419    545 LEELKEKLqLQQLKEELRQLEDRLQELKELLEELRLLRtrkEELEELRERLKELKKKLkeleerLSQLEELLQSLELSEA 624
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162016  558 VAA--QREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEEPTL 622
Cdd:COG0419    625 ENEleEAEEELESELEKLNLQAELEELLQAAL-EELEEKVEELEAEIRRELQRIENEEQLEEKLEEL 690
TACC pfam05010
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins ...
420-593 2.12e-03

Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins TACC 1, 2 and 3 the genes for which are found concentrated in the centrosomes of eukaryotic and may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumor suppressor (AZU-1). The functional homolog (Alp7) in Schizosaccharomyces pombe has been shown to be required for organisation of bipolar spindles.


Pssm-ID: 428254 [Multi-domain]  Cd Length: 201  Bit Score: 40.44  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  420 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVT----KQVSVARQAQVDLEREKKELADSFARV 495
Cdd:pfam05010    8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIeeeqKQKELSHQEIQKVLEEKDQALADLNSV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  496 ---SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQREEELSALRD 571
Cdd:pfam05010   88 eksFSDLFKRYEKQKEVISGYKKNEEVLKKCAQEYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAQAETAALQA 167
                          170       180
                   ....*....|....*....|..
gi 1907162016  572 QLESTQIKLAGAQESMCQQVKD 593
Cdd:pfam05010  168 SLRKEQMKVQSLERTLEQKTKE 189
PRK09039 PRK09039
peptidoglycan -binding protein;
410-570 2.17e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  410 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQaq 478
Cdd:PRK09039    53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ-- 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  479 vdlerekkeladsfarVSDQAQRKtqeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATV 558
Cdd:PRK09039   131 ----------------VSARALAQ-------VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNV 183
                          170
                   ....*....|...
gi 1907162016  559 A-AQREEELSALR 570
Cdd:PRK09039   184 AlAQRVQELNRYR 196
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
353-617 2.20e-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: 42.13  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  353 ERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLG-RQAMDDCEFLRTELDELKRQ-------REDTEK 424
Cdd:pfam12128  386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGELKLRlnqatatPELLLQ 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  425 AQRSLTEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSVARQAQVD--------------------LERE 484
Cdd:pfam12128  466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  485 KKELADSFARVSDQAQ--RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 562
Cdd:pfam12128  544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162016  563 EEELSALRDQLESTQIKLAGAQESM------CQQVKDQRKTLLAGIRKAAEREIQEALSQL 617
Cdd:pfam12128  624 EEQLVQANGELEKASREETFARTALknarldLRRLFDEKQSEKDKKNKALAERKDSANERL 684
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
346-618 2.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 401
Cdd:PRK03918   448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  402 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsvarqaqvDL 481
Cdd:PRK03918   524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELA---DSFARVSDqAQRKTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatv 558
Cdd:PRK03918   591 EERLKELEpfyNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS----- 657
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162016  559 aaqrEEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 618
Cdd:PRK03918   658 ----EEEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
357-612 2.46e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  357 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQqhLGRQAMDDCEFLRTElDELKRQREDTEKAQRSLTEIERKA 436
Cdd:TIGR00606  691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKE-KEIPELRNKLQKVNRDIQRLKNDI 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  437 QANEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------VARQAQVDLER----------EKKELADSFARVSDQ 498
Cdd:TIGR00606  768 EEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqekqEKQHELDTVVSKIEL 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  499 AQRKTQEQQDVLENLKHELatsrQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQ- 577
Cdd:TIGR00606  848 NRKLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQq 923
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1907162016  578 -----IKLAGAQESMCQ-QVKDQRKTL--LAGIRKAAEREIQE 612
Cdd:TIGR00606  924 ekeelISSKETSNKKAQdKVNDIKEKVknIHGYMKDIENKIQD 966
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
282-600 2.55e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 41.80  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  282 HISPVVVIPAEVSSPDSEPVLEKDDLMDMDASQQTLFDNKFDDVFGSSLSSDPFNFNnQNGVNKDEKdhlIERLYREISG 361
Cdd:COG3096    284 HLDQALEFRRELYTSRQQLAAEQYRHVDMSRELAELNGAEGDLEADYQAASDHLNLV-QTALRQQEK---IERYQADLEE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  362 LTGQLDNMKI----------ESQRAMLQLKGRVSELEAELAE-QQHLG---------RQAMDDCEFLRT--ELDELKRQ- 418
Cdd:COG3096    360 LTIRLEEQNEvveeanerqeENEARAEAAELEVDELKSQLADyQQALDvqqtraiqyQQAIAALERAKElcHLPDLTADs 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  419 --------REDTEKAQRSLTEIERKAQANEQRYSKLKEKY------------SELVQNHADLLRKNAE---VTKQVSVAR 475
Cdd:COG3096    440 aeewletfQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYqlvvaiagelarSEAWDVARELLREGPDqrhLAEQVQPLR 519
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  476 QAQVDLER------EKKELADSF---ARVSDQAQR---KTQEQQDVLENLKHELA-------TSRQELQVLHSNLETSAQ 536
Cdd:COG3096    520 MRLSELEQrlrqqqSAERLLADFckrQGKNLDAEEleaLHQELEALIESLSDSVSnareqrmALRQEQEQLQSRIQSLMQ 599
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162016  537 SEAKWLTQIAELEK--EQGSLATVAAQ-----------REEELSALRDQLESTQIKLAGAQESMCQQ--VKDQRKTLLA 600
Cdd:COG3096    600 RAPVWLAAQNALEQlsEQSGEEFTDSQdvteymqqlleREREATVERDELGARKNALDEEIERLSQPggSEDQRLNALA 678
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
340-514 2.58e-03

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227608 [Multi-domain]  Cd Length: 1213  Bit Score: 41.84  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  340 QNGVNKDEKDHLIERLYREISGLTGQLDNMKIE---SQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELK 416
Cdd:COG5283     89 ASKKAYQEYNAQYTQAENKLRSLSGQFGVASEQlmlQQKEIQRLQYAISTLNKSMAAQARLLEQTGNKFGTADAKVVGLR 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  417 -----------RQREDTEKAQRSLTEIERKAQaneQRYS-KLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE 484
Cdd:COG5283    169 esfgrqtealnKQLERTKKVADALTYVLDEAQ---QKLSqALSARLERLQESRTQMSQSSGQLGKRLETDKAGAGALGLL 245
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907162016  485 KKELADSFARVSDQAQRKTQ---EQQDVLENLK 514
Cdd:COG5283    246 GAALAGSFAAIGAAVRRTAQmngELMDKTKQVK 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
328-575 2.82e-03

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: 41.54  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  328 SSLSSDPFNFNNQNGVNKDEKDhlieRLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF 407
Cdd:TIGR04523   99 NKLNSDLSKINSEIKNDKEQKN----KLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLK---EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE 484
Cdd:TIGR04523  171 LENELNLLEKEKLNIQKN---IDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  485 KKE-------LADSFARVSDQAQRKTQE-----------------------------QQDVLENLKHELATSRQELQVLH 528
Cdd:TIGR04523  248 ISNtqtqlnqLKDEQNKIKKQLSEKQKEleqnnkkikelekqlnqlkseisdlnnqkEQDWNKELKSELKNQEKKLEEIQ 327
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907162016  529 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 575
Cdd:TIGR04523  328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
352-455 2.91e-03

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 41.27  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  352 IERLYREISGLTGQldnMKIESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 431
Cdd:COG3206    315 LVALEAQLAELRQQ---IAAELRQILASLPNELALLEQQEAA--------------LEKELAQLKGRLSKLPKLQVQLRE 377
                           90       100
                   ....*....|....*....|....
gi 1907162016  432 IERKAQANEQRYSKLKEKYSELVQ 455
Cdd:COG3206    378 LEREAEAARSLYETLLQRYQELSI 401
PTZ00121 PTZ00121
MAEBL; Provisional
411-619 3.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  411 ELDELKRQREDTEKA---QRSLTEIERKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 487
Cdd:PTZ00121  1303 KADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  488 LADSFA---RVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 564
Cdd:PTZ00121  1382 AAKKKAeekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162016  565 ELSALRDQLESTQIKLAGAQESMCQQVK---DQRKTLLAGIRKAAE-REIQEALSQLEE 619
Cdd:PTZ00121  1462 AKKKAEEAKKADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEaKKKADEAKKAEE 1520
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
411-590 3.43e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  411 ELDELKRQREDTEKAQR-SLTEIERKA-------QANEQRYSKLKEKY-SELVQNHADLLRKNAEVTKQVSVARQAQVDL 481
Cdd:TIGR02794   51 QANRIQQQKKPAAKKEQeRQKKLEQQAeeaekqrAAEQARQKELEQRAaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELADSFARVSDQAQRKTQEqqdvlENLKHELATSRQELQVLHSNLETSAQSEA-------------KWLTQIAEL 548
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEAAKQAEE-----EAKAKAAAEAKKKAEEAKKKAEAEAKAKAeaeakakaeeakaKAEAAKAKA 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907162016  549 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQ 590
Cdd:TIGR02794  206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
443-577 3.74e-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: 40.39  E-value: 3.74e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   443 YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADsfarvsdQAQRKTQEQQDVLENLKHELATSRQ 522
Cdd:smart00787  160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD-------RAKEKLKKLLQEIMIKVKKLEELEE 232
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162016   523 ELQVLHSNLETSAQSEAKWLTQIAELEKeqgSLATVAAQREEELSALRDQLESTQ 577
Cdd:smart00787  233 ELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQ 284
PLN02939 PLN02939
transferase, transferring glycosyl groups
362-553 3.74e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  362 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 434
Cdd:PLN02939   199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  435 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--ARVSDQAQRKTQEQQD 508
Cdd:PLN02939   279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLkeANVSKFSSYKVELLQQ 358
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907162016  509 VLENLKHELATSRQElqvLHSNLETSAQSEAKWLTQIAELEKEQG 553
Cdd:PLN02939   359 KLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKLKEESK 400
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
377-607 3.76e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.19  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  377 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 456
Cdd:PRK10929   111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  457 hADLLRKNAEvtkqvSVARQAQVDlerekkELadsfarvsDQAQRKTQEQQDvLENLKHELATSRQE-----LQVLHSNL 531
Cdd:PRK10929   173 -AQLTALQAE-----SAALKALVD------EL--------ELAQLSANNRQE-LARLRSELAKKRSQqldayLQALRNQL 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  532 ETSAQSEA-KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 607
Cdd:PRK10929   232 NSQRQREAeRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
DUF812 pfam05667
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ...
433-619 3.90e-03

Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.


Pssm-ID: 428574 [Multi-domain]  Cd Length: 601  Bit Score: 41.15  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  433 ERKAQANEQ-RYSKLKEKysELVQNHADLLRKNA--EVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQeqqdv 509
Cdd:pfam05667  221 EWEEEWNSQgLASRLTPE--EYRKRKRTKLLKRIaeQLRSAALASTEATSGASRSKQDLAELLSSFGGSSTTDTN----- 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  510 leNLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKeqgslatvaaQREEELSALRDQLESTQIKLagaqesmcQ 589
Cdd:pfam05667  294 --LTKGSRFTHTEKLQFTNEEAPAATSSPPTKAETEEELQQ----------QREEELEELQEQLEELESSI--------E 353
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907162016  590 QVKDQRKTLLAGIRKAAE--REIQEALSQLEE 619
Cdd:pfam05667  354 ELEKEIKKLESSIKQVEEelEELKEQNEELEK 385
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
409-525 3.97e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 39.92  E-value: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  409 RTELDE-LKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 487
Cdd:pfam00769    8 KQELEErLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQLERELRE 87
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907162016  488 LADSFARVSDQAQRKTQEQqdvlENLKHELATSRQELQ 525
Cdd:pfam00769   88 AQEEVARLEEESERKEEEA----ERLQEELEEAREEEE 121
PRK09039 PRK09039
peptidoglycan -binding protein;
480-585 4.20e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  480 DLEREKKELADSFArvsdQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 559
Cdd:PRK09039    57 RLNSQIAELADLLS----LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
                           90       100
                   ....*....|....*....|....*.
gi 1907162016  560 AQREEELSALRDQLESTQIKLAGAQE 585
Cdd:PRK09039   133 ARALAQVELLNQQIAALRRQLAALEA 158
COG4913 COG4913
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
342-617 4.81e-03

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


Pssm-ID: 227250 [Multi-domain]  Cd Length: 1104  Bit Score: 40.78  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  342 GVNKDEKDHLIERLYREISGLTGQLDNmKIESQRAMLQlkgrvsELEAELAEQQHLGRQAMDDCEF---------LRTEL 412
Cdd:COG4913    611 GSTNDAKVETLRETVKAMLSREDFYMI-KIMRQQGEYI------KLQEQANALAHIQALNFASIDLpsaqrqiaeLQARL 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  413 DELKRQREDTEKAQRSLTEIERKAQANEQRYsklKEKYSELVQNHADLLRKNAEVTKQVSVARQAQvdLEREKKELADSF 492
Cdd:COG4913    684 ERLTHTQSDIAIAKAALDAAQTRQKVLERQY---QQEVTECAGLKKDLKRAAMLSRKVHSIAKQGM--TGALQALGAAHF 758
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  493 ARVSDQAQRKTQEQQD--VLENLKHELATSRQELQVLHSNLeTSAQSEAK--WLTQIAELEKEQGSLATVAAQreeeLSA 568
Cdd:COG4913    759 PQVAPEQHDDIVDIERieHRRQLQKRIDAVNARLRRLREEI-IGRMSDAKkeDTAALSEVGAELDDIPEYLAR----LQT 833
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907162016  569 LRDqlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKaAEREIQEALSQL 617
Cdd:COG4913    834 LTE--DALPEFLARFQELLNRSSDDGVTQLLSHLDH-ERALIEERIEAI 879
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
408-594 4.94e-03

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: 40.77  E-value: 4.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  408 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSelvqnhadllrknaevtkqvsvarqaqvDLEREKK 486
Cdd:TIGR04523  122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYN----------------------------DLKKQKE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  487 ELADSFARVSDQAQRKtqeqQDVLENLKHELAtsrqELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 566
Cdd:TIGR04523  170 ELENELNLLEKEKLNI----QKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
                          170       180
                   ....*....|....*....|....*...
gi 1907162016  567 SALRDQLESTQIKLAGAQESMcQQVKDQ 594
Cdd:TIGR04523  242 NEKTTEISNTQTQLNQLKDEQ-NKIKKQ 268
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
379-547 5.98e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 40.64  E-value: 5.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDelKRQREDTEKAQRSLTEiERKAQANEQRysklkEKYSELVQNHA 458
Cdd:COG3096    517 PLRMRLSELEQRLRQQQSAERLLADFCKRQGKNLD--AEELEALHQELEALIE-SLSDSVSNAR-----EQRMALRQEQE 588
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  459 DLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArvsdQAQRKTQEQQDVLENLKH------ELATSRQELQVLHSNLE 532
Cdd:COG3096    589 QLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFT----DSQDVTEYMQQLLEREREatverdELGARKNALDEEIERLS 664
                          170
                   ....*....|....*
gi 1907162016  533 TSAQSEAKWLTQIAE 547
Cdd:COG3096    665 QPGGSEDQRLNALAE 679
AIP3 smart00806
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ...
344-597 6.27e-03

Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.


Pssm-ID: 214826 [Multi-domain]  Cd Length: 426  Bit Score: 40.04  E-value: 6.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   344 NKDEKDHLIERLYREISGLTGQLDNMK--IESQRAMLQ-LKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELK 416
Cdd:smart00806   72 NVEELDEVKKHIDDEIDTLQNELDEVKqaLESQREAIQrLKERQQNSAANIARpaasPSPVLASSSSAISLANNPDKLNK 151
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   417 RQREDTEKAQRSLTEIeRKAQANEQrySKLKEKYSELVQNHADLLRKNAEVTKQVSVAR--QAQVDLEREKKELADSFAR 494
Cdd:smart00806  152 EQRAELKSLQRELAVL-RQTHNSFF--TEIKESIKDILEKIDKFKSSSLSASGSSNRAYveSSKKKLSEDSDSLLTKVDD 228
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016   495 VSDQ--------AQRKTQEQQDVLENLKHELATSRQELQvlhsNLETSAQSEAKWLTQI--AELEK---EQGSLATvaaq 561
Cdd:smart00806  229 LQDIiealrkdvAQRGVRPSKKQLETVQKELETARKELK----KMEEYIDIEKPIWKKIweAELDKvceEQQFLTL---- 300
                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 1907162016   562 REEELSALRDQLESTQIKLAGAQESMCQQVKDQRKT 597
Cdd:smart00806  301 QEDLIADLKEDLEKAEETFDLVEQCCEEQEKGPSKN 336
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
379-576 6.70e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 223914 [Multi-domain]  Cd Length: 372  Bit Score: 40.08  E-value: 6.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMddceflrtELDELKRQREDTEKAQRSLTEIE----RKAQANEQRYSKLKEKYSELV 454
Cdd:COG0845     72 RVAGIVAEILVKEGDRVKKGQLLA--------RLDPSAVLQAALDQAEAQLARAQallaPAELGDLQREAKLAAEKAAVS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  455 QNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLEnlKHELATSRQELQVLHSNLETS 534
Cdd:COG0845    144 QAELDAAQALLRAAEALVEAAQAALASAKLNLEYTRITAPISGVIGARLVRVGQLVS--AGQALATIADLDPAAALWVLA 221
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907162016  535 AQSEAkwltQIAELEKEQGSLATVAAQREEELSALRDQLEST 576
Cdd:COG0845    222 AVLER----DLLAVKVGQKVTVTLAAGPDQLFAGTVEFISPT 259
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
406-587 6.85e-03

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: 428594 [Multi-domain]  Cd Length: 562  Bit Score: 40.01  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  406 EFLRTELDELKrqrEDTEKAQRSLTEIERK----AQANEQRYSKLKEkysELVQNHADLLRKNaevtKQVSVARQAQVDL 481
Cdd:pfam05701  183 EELTIELIATK---ESLESAHAAHLEAEEHrigaALAREQDKLNWEK---ELKQAEEELQRLN----QQLLSAKDLKSKL 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  482 EREKKELADSFARVSDQAQRKTQEQQDVLENLKHE-------LATSRQELQVLHSNLEtSAQSEAKWLTQIA-----ELE 549
Cdd:pfam05701  253 ETASALLLDLKAELAAYMESKLKEEADGEGNEKKTstsiqaaLASAKKELEEVKANIE-KAKDEVNCLRVAAaslrsELE 331
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907162016  550 KEQGSLATV----------AAQREEELSALRDQLESTQIKLAGAQESM 587
Cdd:pfam05701  332 KEKAELASLrqregmasiaVSSLEAELNRTKSEIALVQAKEKEAREKM 379
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
345-619 7.87e-03

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


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 39.28  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  345 KDEKDHLIERLyREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK 424
Cdd:COG1340     26 KEKRDELRKEA-SELAEKRDELNAKVRELREKAQELREERDEINEEVQELKEKRDEINAKLQELRKEYRELKEKRNEFNL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  425 AQRSLTEIERKAQANE--QRYSKL-KEKYSELVQNHADLLRKNAEVTKQvsvarqaqvdlEREKKELADSFARVsdqaqr 501
Cdd:COG1340    105 GGRSIKSLEREIERLEkkQQTSVLtPEEERELVQKIKELRKELEDAKKA-----------LEENEKLKELKAEI------ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  502 ktQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 581
Cdd:COG1340    168 --DELKKKAREIHEKIQELANEAQEYHEEMIKLFE-------EADELRKEADELHEEFVELSKKIDELHEEFRNLQNELR 238
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907162016  582 GAQesmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG1340    239 ELE----KKIKALRAKEKAAKRREKREELKERAEEIYE 272
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
346-453 8.66e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  346 DEKDHLIERLYREISGLTGQLDNMKIESQR-AMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK 424
Cdd:PRK03918   636 AETEKRLEELRKELEELEKKYSEEEYEELReEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907162016  425 AQRSLTEIER--------KAQANEQRYSKLKEKYSEL 453
Cdd:PRK03918   716 LEKALERVEElrekvkkyKALLKERALSKVGEIASEI 752
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
436-533 9.00e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 39.32  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  436 AQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLErekKELADSFARVSDQAQRKTQEQQDVLENLKH 515
Cdd:TIGR04320  256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQ---KELANAQAQALQTAQNNLATAQAALANAEA 332
                           90
                   ....*....|....*...
gi 1907162016  516 ELATSRQELQVLHSNLET 533
Cdd:TIGR04320  333 RLAKAKEALANLNADLAK 350
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
379-608 9.54e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 39.89  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  379 QLKGRVSELEAELAEQQHLGRQAMDdceflrTELDELKRQREDTEKAQRSL--------TEIERKAQANEQRYSKLKEKY 450
Cdd:pfam15964  364 ELERQKERLEKELASQQEKRAQEKE------ALRKEMKKEREELGATMLALsqnvaqleAQVEKVTREKNSLVSQLEEAQ 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  451 SELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSN 530
Cdd:pfam15964  438 KQLASQEMDVTKVCGEMRYQLN---QTKMKKDEAEKEHREYRTKTGRQLEIKDQE----IEKLGLELSESKQRLEQAQQD 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162016  531 lETSAQSEAKWLTQ----------IAELEKEQ---------GSLATVAAQREEELS-------ALRDQLESTQIKLAGAQ 584
Cdd:pfam15964  511 -AARAREECLKLTEllgesehqlhLTRLEKESiqqsfsneaKAQALQAQQREQELTqkmqqmeAQHDKTVNEQYSLLTSQ 589
                          250       260
                   ....*....|....*....|....
gi 1907162016  585 ESMCQQVKDQRKTLLAGIRKAAER 608
Cdd:pfam15964  590 NTFIAKLKEECCTLAKKLEEITQK 613
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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