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Conserved domains on  [gi|312176405|ref|NP_001185898|]
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intersectin-2 isoform 3 [Mus musculus]

Protein Classification

EH domain-containing protein( domain architecture ID 12184509)

EH (Eps15 homology) domain-containing protein contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+; similar to Saccharomyces cerevisiae protein TAX4, which negatively regulates signaling through the cell integrity pathway

CATH:  1.10.238.10
Gene Ontology:  GO:0005515|GO:0005509
PubMed:  11911876|9397678|7568168
SCOP:  4000946

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 15-107 1.89e-34

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 125.85  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405    15 MWAITSEERTKHDKQFDNLKPSG-GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQGQ 93
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQdGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....
gi 312176405    94 QLPVVLPPIMKQPP 107
Cdd:smart00027  81 PIPASLPPSLIPPS 94
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 238-317 4.77e-29

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 110.83  E-value: 4.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   238 EWAVPQPSRLKYRQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLTDMAKAGQ 317
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 349-607 2.82e-09

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.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 60.37  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   349 QKTQEEEPQKKLPVTFEDKRKANYErgNMELEKRRQVLMEQQQREAERKAQKEKEEWE-------RKQRELQEQEWKKQL 421
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIID--LEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllylDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   422 ELEKRLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNG 501
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   502 KHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQ-----LLNERIKNMQLSNTPD 576
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESerlssAAKLKEEELELKSEEE 404

                          250       260       270
                   ....*....|....*....|....*....|.
gi 312176405   577 SGISLLHKKSSEKEELCQRLKEQLDALEKET 607
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEELEILEEE 435
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 86-196 3.13e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   86 IKLKLQGQQLPVvlPPImkQPPMFSPLISARFGMGSMPNLSIHQPLPPVAPIAtPLSSATSGtsiPPLMMPAPLVPSVST 165
Cdd:pfam03154 415 LQLMPQSQQLPP--PPA--QPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFP-QHPFVPGG---PPPITPPSGPPTSTS 486

                          90       100       110
                  ....*....|....*....|....*....|..
gi 312176405  166 SSLPngtaSLIQPLSIPYSSS-TLPHASSYSL 196
Cdd:pfam03154 487 SAMP----GIQPPSSASVSSSgPVPAAVSCPL 514
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 15-107 1.89e-34

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 125.85  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405    15 MWAITSEERTKHDKQFDNLKPSG-GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQGQ 93
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQdGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....
gi 312176405    94 QLPVVLPPIMKQPP 107
Cdd:smart00027  81 PIPASLPPSLIPPS 94
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 238-317 4.77e-29

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 110.83  E-value: 4.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   238 EWAVPQPSRLKYRQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLTDMAKAGQ 317
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 249-315 1.89e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 1.89e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405 249 YRQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLTDMAKA 315
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 27-91 8.88e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 94.98  E-value: 8.88e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176405  27 DKQFDNLKPSG-GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQ 91
Cdd:cd00052    2 DQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 30-86 1.52e-13

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 67.01  E-value: 1.52e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   30 FDNLKPSGGYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLI 86
Cdd:pfam12763  16 FSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 248-310 1.04e-12

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 64.70  E-value: 1.04e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176405  248 KYRQKFNSLDKGmSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLT 310
Cdd:pfam12763  11 KYWEIFSGLKPE-NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 349-607 2.82e-09

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: 60.37  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   349 QKTQEEEPQKKLPVTFEDKRKANYErgNMELEKRRQVLMEQQQREAERKAQKEKEEWE-------RKQRELQEQEWKKQL 421
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIID--LEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllylDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   422 ELEKRLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNG 501
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   502 KHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQ-----LLNERIKNMQLSNTPD 576
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESerlssAAKLKEEELELKSEEE 404

                          250       260       270
                   ....*....|....*....|....*....|.
gi 312176405   577 SGISLLHKKSSEKEELCQRLKEQLDALEKET 607
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEELEILEEE 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-613 3.30e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLmeQQQREAERKAQKEKEEWERKQRELQEQEWK-----KQLELEKRLEKQRELERQREEERRKEIERREAAK 452
Cdd:COG1196  197 ELERQLEPL--ERQAEKAERYRELKEELKELEAELLLLKLReleaeLEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 453 QELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCD 532
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 533 LEIMEIKQLQQELKEYQNKLIYLvpEKQLLNERIKNMQLSNTpdsgISLLHKKSSEKEELCQRLKEQLDALEKETASKLS 612
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEA--EEELEELAEELLEALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEE 428


                 .
gi 312176405 613 E 613
Cdd:COG1196  429 A 429
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 378-609 1.96e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   378 ELEKRRQVLMEQQQREAERKAQKEkEEWERKQRELQEQEWKKQlELEKRLEKQRELERQREeerrkeierreAAKQELER 457
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLE-----------EALNDLEA 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   458 QRRLEWERLRRQELLSQKT--REQEDIVR-LSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQcdle 534
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKLEEevSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---- 862

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   535 imeIKQLQQELKEYQNKLIYLVPEKQLLNERIKNM--QLSNTpDSGISLLHKKSSEKEELCQRLKEQLDALEKETAS 609
Cdd:TIGR02169  863 ---KEELEEELEELEAALRDLESRLGDLKKERDELeaQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
PTZ00121 PTZ00121
MAEBL; Provisional
 349-614 9.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  349 QKTQEEEPQKKLpvtfEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLE 428
Cdd:PTZ00121 1468 EAKKADEAKKKA----EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  429 KQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLE----LEAVNGKHQ 504
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  505 QISGRLQDVQIRKQTQKTELEVLDKQCDL----EIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSNTPDSGIS 580
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703

                         250       260       270
                  ....*....|....*....|....*....|....
gi 312176405  581 LLHKKSSEKEElcQRLKEQLDALEKETASKLSEM 614
Cdd:PTZ00121 1704 AEELKKKEAEE--KKKAEELKKAEEENKIKAEEA 1735
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
250-308 1.11e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312176405 250 RQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMH 308
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 86-196 3.13e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   86 IKLKLQGQQLPVvlPPImkQPPMFSPLISARFGMGSMPNLSIHQPLPPVAPIAtPLSSATSGtsiPPLMMPAPLVPSVST 165
Cdd:pfam03154 415 LQLMPQSQQLPP--PPA--QPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFP-QHPFVPGG---PPPITPPSGPPTSTS 486

                          90       100       110
                  ....*....|....*....|....*....|..
gi 312176405  166 SSLPngtaSLIQPLSIPYSSS-TLPHASSYSL 196
Cdd:pfam03154 487 SAMP----GIQPPSSASVSSSgPVPAAVSCPL 514
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
38-84 4.96e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 312176405  38 GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMK 84
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
PTZ00184 PTZ00184
calmodulin; Provisional
 248-307 5.21e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 5.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405 248 KYRQKFNSLDKGMSGYLSGFQARNAL--LQSNLSQTQLATIWTLADIDGDGQLKAEEFILAM 307
Cdd:PTZ00184  85 EIKEAFKVFDRDGNGFISAAELRHVMtnLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 15-107 1.89e-34

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 125.85  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405    15 MWAITSEERTKHDKQFDNLKPSG-GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQGQ 93
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQdGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....
gi 312176405    94 QLPVVLPPIMKQPP 107
Cdd:smart00027  81 PIPASLPPSLIPPS 94
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 238-317 4.77e-29

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 110.83  E-value: 4.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   238 EWAVPQPSRLKYRQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLTDMAKAGQ 317
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 249-315 1.89e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 1.89e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405 249 YRQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLTDMAKA 315
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 27-91 8.88e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 94.98  E-value: 8.88e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176405  27 DKQFDNLKPSG-GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQ 91
Cdd:cd00052    2 DQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 30-86 1.52e-13

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 67.01  E-value: 1.52e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   30 FDNLKPSGGYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLI 86
Cdd:pfam12763  16 FSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 248-310 1.04e-12

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 64.70  E-value: 1.04e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176405  248 KYRQKFNSLDKGmSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMHLT 310
Cdd:pfam12763  11 KYWEIFSGLKPE-NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 349-607 2.82e-09

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: 60.37  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   349 QKTQEEEPQKKLPVTFEDKRKANYErgNMELEKRRQVLMEQQQREAERKAQKEKEEWE-------RKQRELQEQEWKKQL 421
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIID--LEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllylDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   422 ELEKRLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNG 501
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   502 KHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQ-----LLNERIKNMQLSNTPD 576
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESerlssAAKLKEEELELKSEEE 404

                          250       260       270
                   ....*....|....*....|....*....|.
gi 312176405   577 SGISLLHKKSSEKEELCQRLKEQLDALEKET 607
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEELEILEEE 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-613 3.30e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLmeQQQREAERKAQKEKEEWERKQRELQEQEWK-----KQLELEKRLEKQRELERQREEERRKEIERREAAK 452
Cdd:COG1196  197 ELERQLEPL--ERQAEKAERYRELKEELKELEAELLLLKLReleaeLEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 453 QELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCD 532
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 533 LEIMEIKQLQQELKEYQNKLIYLvpEKQLLNERIKNMQLSNTpdsgISLLHKKSSEKEELCQRLKEQLDALEKETASKLS 612
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEA--EEELEELAEELLEALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEE 428


                 .
gi 312176405 613 E 613
Cdd:COG1196  429 A 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 364-570 1.21e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 364 FEDKRKANYERGN--MELEKRRQVLMEQQQREAERKAQ--KEKEEWERKQRELQEQ--EWKKQLE---------LEKRLE 428
Cdd:COG1196  283 LEEAQAEEYELLAelARLEQDIARLEERRRELEERLEEleEELAELEEELEELEEEleELEEELEeaeeeleeaEAELAE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 429 KQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISG 508
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405 509 RLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQ 570
Cdd:COG1196  443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 378-609 1.96e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   378 ELEKRRQVLMEQQQREAERKAQKEkEEWERKQRELQEQEWKKQlELEKRLEKQRELERQREeerrkeierreAAKQELER 457
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLE-----------EALNDLEA 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   458 QRRLEWERLRRQELLSQKT--REQEDIVR-LSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQcdle 534
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKLEEevSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---- 862

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   535 imeIKQLQQELKEYQNKLIYLVPEKQLLNERIKNM--QLSNTpDSGISLLHKKSSEKEELCQRLKEQLDALEKETAS 609
Cdd:TIGR02169  863 ---KEELEEELEELEAALRDLESRLGDLKKERDELeaQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-613 6.33e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEwKKQLELEKRLEKQRELERQREEERRKEIERREAAKQELER 457
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELE-AELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 458 -QRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIM 536
Cdd:COG1196  300 lEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405 537 EIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLsntpdsgisLLHKKSSEKEELCQRLKEQLDALEKETASKLSE 613
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLE---------RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 350-622 9.12e-08

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: 9.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   350 KTQEEEPQKKLPVTFEDKRKANYERGNMELEKrrqvlMEQQQREAERKAQKEKEEWERKQRELQEQEwKKQLELEKRL-- 427
Cdd:TIGR02168  219 KAELRELELALLVLRLEELREELEELQEELKE-----AEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   428 --EKQRELERQREEerrkeierreaAKQELER-QRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQ 504
Cdd:TIGR02168  293 laNEISRLEQQKQI-----------LRERLANlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   505 QISGRLQDVQIRKQTQKTELEVLDKqcdleimEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQlsntpdSGISLLHK 584
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRS-------KVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLK 428

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 312176405   585 KSSEKEElcQRLKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:TIGR02168  429 KLEEAEL--KELQAELEELEEELEELQEELERLEEALE 464
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 377-613 6.62e-07

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: 52.67  E-value: 6.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   377 MELEKRRQVLMEQQQREA-------ERKAQKEKEEWERKQrELQEQEWKKQLELEKRLEKQRELERQREEERRKEIERRE 449
Cdd:pfam02463  169 RKKKEALKKLIEETENLAeliidleELKLQELKLKEQAKK-ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   450 AAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQ-KTELEVLD 528
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   529 KQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERiknMQLSNTPDSGISLLHKKSSEKEELCQRLKEQLDALEKETA 608
Cdd:pfam02463  328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404


                   ....*
gi 312176405   609 SKLSE 613
Cdd:pfam02463  405 KEAQL 409
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 388-622 4.43e-06

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: 50.02  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  388 EQQQREAERKAQKEKEEWERKQRELQEQEWKKQlELEKRLEKQRELERQREEERRKEIERreaaKQELERQRrlewerlr 467
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQIN-DLESKIQNQEKLNQQKDEQIKKLQQE----KELLEKEI-------- 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  468 rQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKE 547
Cdd:TIGR04523 429 -ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176405  548 YQNKLIYLVPEKQLLNERIKnmQLSNTPDSGISLLHKKSSEKEELCQRLKEqlDALEKETASK---LSEMDSFNNQLK 622
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIE--KLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKnkeIEELKQTQKSLK 581
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 378-621 6.85e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 6.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   378 ELEKRRQVLMEQQQREAErkAQKEKEEWERKQRELQEQEWKKQLELEkrlekqrelerqreEERRKEIERREAAKQELER 457
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAE--LEKALAELRKELEELEEELEQLRKELE--------------ELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   458 QRRLEWERLRRQELLsqkTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIME 537
Cdd:TIGR02168  742 VEQLEERIAQLSKEL---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   538 IKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSntpdsgISLLHKKSSEKEELCQRLKEQLDALEKETASKLSEMDSF 617
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSED------IESLAAEIEELEELIEELESELEALLNERASLEEALALL 892


                   ....
gi 312176405   618 NNQL 621
Cdd:TIGR02168  893 RSEL 896
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 349-545 1.10e-05

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: 48.58  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  349 QKTQEEEPQKKLPVTFEDKRKANYERGNMElEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKrle 428
Cdd:pfam17380 404 VKILEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL--- 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  429 kqrelERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKslhlELEAVNGKHQQISG 508
Cdd:pfam17380 480 -----EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR----EAEEERRKQQEMEE 550

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 312176405  509 RLQ-DVQIRKQT-QKTELEVLDKQCDL--EIMEIKQLQQEL 545
Cdd:pfam17380 551 RRRiQEQMRKATeERSRLEAMEREREMmrQIVESEKARAEY 591
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 378-622 1.32e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   378 ELEKRRQVLMEQQQ--REAERKAQKEKEEWERKQRELQEQEWKKQLELEKrlekqrelerqrEEERRKEIERREAAKQEL 455
Cdd:TIGR02168  695 ELEKALAELRKELEelEEELEQLRKELEELSRQISALRKDLARLEAEVEQl----------eERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   456 ERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRkqtqkteLEVLDKQCDLEI 535
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-------LESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   536 MEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQlsntpdSGISLLHKKSSEKEELCQRLKEQLDALEKETASKLSEMD 615
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELE------SELEALLNERASLEEALALLRSELEELSEELRELESKRS 911


                   ....*..
gi 312176405   616 SFNNQLK 622
Cdd:TIGR02168  912 ELRRELE 918
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 366-567 1.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 366 DKRKANYERGNMELEKRRQVLMEQQQR--EAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLEKQRELERQREEERRK 443
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 444 EIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTE 523
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 312176405 524 LEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIK 567
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 337-544 5.91e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  337 QVDSVNGTLPSYQKTQEEEPQKKLPVTFEdKRKANYERGNMELEKRRQVLMEQQQREAE--RKAQKEKEEWERKQRELQE 414
Cdd:pfam15709 301 QTFVVTGNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERAEMRRLEVERKRREQEeqRRLQQEQLERAEKMREELE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  415 QEWKKQLElEKRLEKQREL-ERQREEERRKEIERREAAKQELERQrRLEWERLRRQELlsQKTREQEDIVRLSSRKKSLH 493
Cdd:pfam15709 380 LEQQRRFE-EIRLRKQRLEeERQRQEEEERKQRLQLQAAQERARQ-QQEEFRRKLQEL--QRKKQQEEAERAEAEKQRQK 455

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312176405  494 LELEAVNGKHQQISGRLQDVQIRKQTQKTELEvldKQCDLEIMEIKQLQQE 544
Cdd:pfam15709 456 ELEMQLAEEQKRLMEMAEEERLEYQRQKQEAE---EKARLEAEERRQKEEE 503
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 485-622 8.02e-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: 45.97  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  485 LSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLiyLVPEKQL--L 562
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQL--RDKDKQLagL 420

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312176405  563 NERIKNMQL-SNTPDSGISLLHKKSSEKEELCQRLKEQLDALEKEtasKLSEMDSFNNQLK 622
Cdd:pfam10174 421 KERVKSLQTdSSNTDTALTTLEEALSEKERIIERLKEQREREDRE---RLEELESLKKENK 478
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 365-430 9.14e-05

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 44.87  E-value: 9.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176405  365 EDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKrlEKQ 430
Cdd:pfam07946 257 EALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKER--KKE 320
PTZ00121 PTZ00121
MAEBL; Provisional
 349-614 9.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  349 QKTQEEEPQKKLpvtfEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLE 428
Cdd:PTZ00121 1468 EAKKADEAKKKA----EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  429 KQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLE----LEAVNGKHQ 504
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAE 1623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  505 QISGRLQDVQIRKQTQKTELEVLDKQCDL----EIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSNTPDSGIS 580
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703

                         250       260       270
                  ....*....|....*....|....*....|....
gi 312176405  581 LLHKKSSEKEElcQRLKEQLDALEKETASKLSEM 614
Cdd:PTZ00121 1704 AEELKKKEAEE--KKKAEELKKAEEENKIKAEEA 1735
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
250-308 1.11e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312176405 250 RQKFNSLDKGMSGYLSGFQARNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMH 308
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 453-622 1.59e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   453 QELERQRRLEWERLRRQELLSQKTREQEDIVRLSS--RKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQ 530
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   531 cDLEI-MEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSNTPDSGISLLHKKSS-EKEELCQRLKEQLDALEKETA 608
Cdd:TIGR02168  276 -VSELeEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKLEELKEELE 354

                          170
                   ....*....|....
gi 312176405   609 SKLSEMDSFNNQLK 622
Cdd:TIGR02168  355 SLEAELEELEAELE 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 351-622 1.72e-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: 45.06  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   351 TQEEEPQKKLPVTFEDKrKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEwkkqlELEKRLEKQ 430
Cdd:TIGR02169  740 EELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE-----EEVSRIEAR 813

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   431 RELERQREEERRKEIERREAAKQELERQRRlewerlrrqELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRL 510
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRI---------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   511 QD--------------VQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVP-------------EKQLLN 563
Cdd:TIGR02169  885 GDlkkerdeleaqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqaELQRVE 964

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405   564 ERIKNMQLSNTpdsgisllhKKSSEKEELCQR---LKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:TIGR02169  965 EEIRALEPVNM---------LAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEYEKKKR 1017
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 378-622 2.02e-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: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   378 ELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQlELEKRLEKQRELERQREEERRKEIERREAAKQ---- 453
Cdd:TIGR02169  219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekig 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   454 ----ELERQRRLEWERLRRQELLSQKTRE-QEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLD 528
Cdd:TIGR02169  298 eleaEIASLERSIAEKERELEDAEERLAKlEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   529 KQCDLEIMEIKQLQQELKEYQNKL-------IYLVPEKQLLNERIKNMQLS--------NTPDSGISLLHKKSSEKEELC 593
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAiagieakiNELEEEKEDKALEIKKQEWKL 457

                          250       260
                   ....*....|....*....|....*....
gi 312176405   594 QRLKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELS 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-615 2.16e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLmEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLEKQRELERQREEERRKEIERREAAKQELER 457
Cdd:COG1196  250 ELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 458 QRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIME 537
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176405 538 IKQLQQELKEYQNKLIYLvpEKQLLNERIKNMQLSNTpdsgISLLHKKSSEKEELCQRLKEQLDALEKETASKLSEMD 615
Cdd:COG1196  409 EEALLERLERLEEELEEL--EEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 378-616 2.86e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  378 ELEKRRQVLME-----QQQREAERKAQK-EKEEWERKQRELQEQEWKKQLELEKRLEKQrELERQREEERRKEIERREAA 451
Cdd:pfam07888  38 ECLQERAELLQaqeaaNRQREKEKERYKrDREQWERQRRELESRVAELKEELRQSREKH-EELEEKYKELSASSEELSEE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  452 KQELERQrrlewerlrrQELLSQKTRE-QEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKq 530
Cdd:pfam07888 117 KDALLAQ----------RAAHEARIRElEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  531 cdleimEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSNTPdsgislLHKKSSEKEELCQRLK---EQLDALEKET 607
Cdd:pfam07888 186 ------ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT------AHRKEAENEALLEELRslqERLNASERKV 253

                         250
                  ....*....|..
gi 312176405  608 A---SKLSEMDS 616
Cdd:pfam07888 254 EglgEELSSMAA 265
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 86-196 3.13e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   86 IKLKLQGQQLPVvlPPImkQPPMFSPLISARFGMGSMPNLSIHQPLPPVAPIAtPLSSATSGtsiPPLMMPAPLVPSVST 165
Cdd:pfam03154 415 LQLMPQSQQLPP--PPA--QPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFP-QHPFVPGG---PPPITPPSGPPTSTS 486

                          90       100       110
                  ....*....|....*....|....*....|..
gi 312176405  166 SSLPngtaSLIQPLSIPYSSS-TLPHASSYSL 196
Cdd:pfam03154 487 SAMP----GIQPPSSASVSSSgPVPAAVSCPL 514
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
378-566 4.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLMEQQQREAE-RKAQKEKEEWERKQRELQEQEWKKQLELEkRLEKQRELERQREEERrkeierreAAKQEL- 455
Cdd:COG4717   72 ELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELE--------ALEAELa 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 456 ---ERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKH-QQISGRLQDVQIRKQTQKTELEVLDKqc 531
Cdd:COG4717  143 elpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQE-- 220

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 312176405 532 dleimEIKQLQQELKEYQNKLIYLVPEKQLLNERI 566
Cdd:COG4717  221 -----ELEELEEELEQLENELEAAALEERLKEARL 250
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 368-430 4.91e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 4.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176405 368 RKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEW-ERKQRELQEQEWKKQLELEKRLEKQ 430
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAAL 129
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
382-609 7.26e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  382 RRQVLMEQQQREAERKAQKEKEEWERKQRELQEQE--------WKKQLELEkrlekqrelerqreeerrkeierreAAKQ 453
Cdd:COG4913   241 HEALEDAREQIELLEPIRELAERYAAARERLAELEylraalrlWFAQRRLE-------------------------LLEA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  454 ELERqrrlewerlrrqeLLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRlqdvqiRKQTQKTELEVLDKqcdl 533
Cdd:COG4913   296 ELEE-------------LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLER---- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  534 eimEIKQLQQELKEYQNKLIYL---VP--EKQLLNERIKNMQLSNTPDSGISLLHKKSSEKEELCQRLKEQLDALEKETA 608
Cdd:COG4913   353 ---ELEERERRRARLEALLAALglpLPasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429


                  .
gi 312176405  609 S 609
Cdd:COG4913   430 S 430
EF-hand_7 pfam13499
EF-hand domain pair;
248-307 8.03e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 8.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312176405  248 KYRQKFNSLDKGMSGYLSG--FQA--RNALLQSNLSQTQLATIWTLADIDGDGQLKAEEFILAM 307
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVeeLKKllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
PTZ00121 PTZ00121
MAEBL; Provisional
 354-622 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  354 EEPQKKLpvtfEDKRKANYERGNMELEKRRQVLMEQQQR-------EAERKAQK-EKEEWERKQRELQEQEWKKQLELEK 425
Cdd:PTZ00121 1233 EEAKKDA----EEAKKAEEERNNEEIRKFEEARMAHFARrqaaikaEEARKADElKKAEEKKKADEAKKAEEKKKADEAK 1308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  426 RLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDivrlssRKKSLHLELEAVNGKHQQ 505
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE------KAEAAEKKKEEAKKKADA 1382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  506 ISGRLQDVQIRKQTQKTELEvlDKQCDLEIMEIKQLQQELKEYQNKliylVPEKQLLNERIKNMQLSNTPDSgislLHKK 585
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKKK----AEEKKKADEAKKKAEEAKKADE----AKKK 1452

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 312176405  586 SSEKEELCQRLKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 348-571 1.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   348 YQKTQEEEPQKKLPVTFEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKkqlELEKRL 427
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA---EAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   428 EKQRELERQREEERRKEIERREAAKQELER-QRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQ- 505
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEl 864

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405   506 ------ISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLiylvpekQLLNERIKNMQL 571
Cdd:TIGR02168  865 eelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLEL 929
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 389-555 1.55e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   389 QQQREAERKAQKEKEEWERKQRELQEQeWKKQLELEKRLEKQRELERQREEERRKEIERREAAKQELERQRrlewerlrr 468
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------- 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   469 QELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQK--------TELEVLDKQCDLEIMEIKQ 540
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEE 969

                          170
                   ....*....|....*
gi 312176405   541 LQQELKEYQNKLIYL 555
Cdd:TIGR02168  970 ARRRLKRLENKIKEL 984
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 347-573 1.92e-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: 41.50  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   347 SYQKTQEEEPQKKLPVTFEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKR 426
Cdd:pfam02463  289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   427 LEKQRELERQREEERRKEIERREAAKQELERQrrleweRLRRQELLSQKTREQEDIVRLSSRKKSLhLELEAVNGKhqqi 506
Cdd:pfam02463  369 EQLEEELLAKKKLESERLSSAAKLKEEELELK------SEEEKEAQLLLELARQLEDLLKEEKKEE-LEILEEEEE---- 437

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   507 sgRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLvpEKQLLNERIKNMQLSN 573
Cdd:pfam02463  438 --SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE--QLELLLSRQKLEERSQ 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 364-570 1.98e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   364 FEDKRKANYERGNmelEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEkRLEKQRELERQREEERRK 443
Cdd:TIGR02168  283 IEELQKELYALAN---EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA-ELEEKLEELKEELESLEA 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   444 EIERREAAKQELERQRRLEW---ERLRRQ--ELLSQKTREQEDIVRLSSRKKSL-------HLELEAVNGKHQqiSGRLQ 511
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEeqlETLRSKvaQLELQIASLNNEIERLEARLERLedrrerlQQEIEELLKKLE--EAELK 436

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 312176405   512 DVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQ 570
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
336-618 2.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 336 KQVDSVNGTLPSYQKTQEEEPQKKLPVTFEDKRKANYERGNMELEKRRQVLMEQ----QQREAERKAQKEKEEWERKQRE 411
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieelEEKVKELKELKEKAEEYIKLSE 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 412 LQEQEWKKQLELEKRL----------EKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTR---- 477
Cdd:PRK03918 301 FYEEYLDELREIEKRLsrleeeingiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkr 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 478 ----EQEDIVR----LSSRKKSLHLELEAVNGKH---QQISGRLQDVQIRKQTQKTELEV----LDKQCDLEIM-----E 537
Cdd:PRK03918 381 ltglTPEKLEKeleeLEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVcgreLTEEHRKELLeeytaE 460

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 538 IKQLQQELKEYQNKL-----------IYLVPEKQLLNERIKNMQLSNTPDSGISLLHKKSSEKEELCQRLKEQLDALEKE 606
Cdd:PRK03918 461 LKRIEKELKEIEEKErklrkelreleKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE 540

                        330
                 ....*....|..
gi 312176405 607 TASKLSEMDSFN 618
Cdd:PRK03918 541 IKSLKKELEKLE 552
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 365-613 2.35e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   365 EDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQ---RELQEQEWKKQLELEKRLEKQRELERQREEER 441
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQallKEKREYEGYELLKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   442 RKEIERREAAKQELE----------RQRRLEWERLRRQELLSQKTR------EQEDIVR-----------LSSRKKSLHL 494
Cdd:TIGR02169  250 EEELEKLTEEISELEkrleeieqllEELNKKIKDLGEEEQLRVKEKigeleaEIASLERsiaekereledAEERLAKLEA 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   495 ELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQlsNT 574
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK--RE 407

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 312176405   575 PDSGISLLHKKSSEKEELCQ---RLKEQLDALEKETASKLSE 613
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAaiaGIEAKINELEEEKEDKALE 449
PTZ00121 PTZ00121
MAEBL; Provisional
 347-551 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  347 SYQKTQEEEPQKKLpvtfEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQL-ELEK 425
Cdd:PTZ00121 1298 AEEKKKADEAKKKA----EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKK 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  426 RLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQ 505
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA 1453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 312176405  506 ISGRLQDVQIRKQTQKTELEVLDKQCDlEIMEIKQLQQELKEYQNK 551
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKKKAEEAKKK 1498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 469-608 3.85e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 469 QELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQcdleimeIKQLQQELKEy 548
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAELRAELEA- 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312176405 549 qnkliylvpEKQLLNERIKNMQLSNTPDSGISLLHKKSSEK--------EELCQRLKEQLDALEKETA 608
Cdd:COG4942  102 ---------QKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLA 160
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 248-308 3.93e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 3.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312176405 248 KYRQKFNSLDKGMSGYLSGFQARNAL--LQSNLSQTQLATIWTLADIDGDGQLKAEEFILAMH 308
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 250-312 4.26e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 38.35  E-value: 4.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405 250 RQKFNSLDKGMSGYLSGFQARNALLQSNL--SQTQLATIWTLADIDGDGQLKAEEFiLAMH--LTDM 312
Cdd:cd16185    3 RQWFRAVDRDRSGSIDVNELQKALAGGGLlfSLATAEKLIRMFDRDGNGTIDFEEF-AALHqfLSNM 68
Oxysterol_BP pfam01237
Oxysterol-binding protein;
354-408 4.81e-03

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 39.83  E-value: 4.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405  354 EEPQKKLPVTfeDKR----KANYERGNMEL---EKRRqvlMEQQQREAERKAQKEKEEWERK 408
Cdd:pfam01237 283 TDELGKLPPT--DSRlrpdQRALENGDIDEaeeEKLR---LEEKQRARRKEREEKGEEWKPR 339
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
38-84 4.96e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 312176405  38 GYITGDQARTFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMK 84
Cdd:COG5126   84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
PTZ00184 PTZ00184
calmodulin; Provisional
 248-307 5.21e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 5.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312176405 248 KYRQKFNSLDKGMSGYLSGFQARNAL--LQSNLSQTQLATIWTLADIDGDGQLKAEEFILAM 307
Cdd:PTZ00184  85 EIKEAFKVFDRDGNGFISAAELRHVMtnLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
349-429 5.48e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.64  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 349 QKTQEEEPQKKLPVTFEDKRKAN--YERGNMELEKRRQVLMEQQqREAERKAQKEKEEWERKQRELQEQEWKKQLELEKR 426
Cdd:COG3064    7 EKAAEAAAQERLEQAEAEKRAAAeaEQKAKEEAEEERLAELEAK-RQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85


                 ...
gi 312176405 427 LEK 429
Cdd:COG3064   86 AAE 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-562 6.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 378 ELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLEKQRELERQREEERRKEIERREAAKQELER 457
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 458 QRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIME 537
Cdd:COG1196  418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497

                        170       180
                 ....*....|....*....|....*
gi 312176405 538 IKQLQQELKEYQNKLIYLVPEKQLL 562
Cdd:COG1196  498 EAEADYEGFLEGVKAALLLAGLRGL 522
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 388-572 6.43e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 388 EQQQREAE---RKAQKEKEEWERKQRELQEQEWKKQLELEKRLEKQrelerqreeeRRKEIERREAAKQELErQRRLEWE 464
Cdd:PRK00409 526 EELERELEqkaEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA----------EKEAQQAIKEAKKEAD-EIIKELR 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 465 RLRRQELLSQKTREQEDIvrlssrKKSLHLELEAVNgKHQQISGRLQD-------VQIRKQTQKTE-LEVLDK---QCDL 533
Cdd:PRK00409 595 QLQKGGYASVKAHELIEA------RKRLNKANEKKE-KKKKKQKEKQEelkvgdeVKYLSLGQKGEvLSIPDDkeaIVQA 667

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312176405 534 EIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLS 572
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLE 706
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 379-558 6.48e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.60  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  379 LEKRRQV--LMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLElEKRLEKQRELERQREEE----------RRKEIE 446
Cdd:pfam05262 194 VNFRRDMtdLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFA-QDNADKQRDEVRQKQQEaknlpkpadtSSPKED 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  447 RREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVR--LSSRKKSLHLELEAvNGKHQQISGRLQDVQIRKQTQKTE- 523
Cdd:pfam05262 273 KQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQesKASEKEAEDKELEA-QKKREPVAEDLQKTKPQVEAQPTSl 351

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312176405  524 -------------LEVLDKQCDLEIMEIKQLQQE-------LKEYQNKLIYLVPE 558
Cdd:pfam05262 352 nedaidssnpvygLKVVDPITNLSELVLIDLKTEvrlresaQQTIRRRGLYEREK 406
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 354-616 6.69e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   354 EEPQKKLPVTFEDKRKANYER-------GNMElEKRRQVLMEQQQREAERKAQKE--KEEWERK----------QRELQE 414
Cdd:pfam15921  345 EELEKQLVLANSELTEARTERdqfsqesGNLD-DQLQKLLADLHKREKELSLEKEqnKRLWDRDtgnsitidhlRRELDD 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   415 QEWKKQlelekRLEKQRELERQREEERRKEIERREAAKQE-LERQRRLEWERLRRQELLSQKTREqedivrLSSRKkslh 493
Cdd:pfam15921  424 RNMEVQ-----RLEALLKAMKSECQGQMERQMAAIQGKNEsLEKVSSLTAQLESTKEMLRKVVEE------LTAKK---- 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   494 LELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQN------KLIYLVPEK----QLLN 563
Cdd:pfam15921  489 MTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqteceALKLQMAEKdkviEILR 568

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 312176405   564 ERIKNM-QL--SNTPDSGISLLHKKSSEKEELCQRLK-EQLDALEKETASKLSEMDS 616
Cdd:pfam15921  569 QQIENMtQLvgQHGRTAGAMQVEKAQLEKEINDRRLElQEFKILKDKKDAKIRELEA 625
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 348-622 6.78e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  348 YQKTQEEEPQkklpvtFEDKRKANYERGNMELEKRRQVL-MEQQQREAERKAQKEKEEWERKQRELQeqewKKQLELEKr 426
Cdd:pfam05483 327 CQLTEEKEAQ------MEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRLEKNEDQLKIITMELQ----KKSSELEE- 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  427 lekqrelerQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLH---LELEAVNGKH 503
Cdd:pfam05483 396 ---------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHdleIQLTAIKTSE 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  504 QQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQ-------ELKEYQNKLIYLVPEKQLLNERIKNMQLSNTpd 576
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlELKKHQEDIINCKKQEERMLKQIENLEEKEM-- 544

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 312176405  577 sgiSLLHKKSSEKEELCQR---LKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:pfam05483 545 ---NLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQMK 590
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 368-532 6.86e-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: 39.82  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   368 RKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKR-LEKQRELERQREEERRKEIE 446
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLeFNEEEYRLKSRLGELKLRLN 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   447 RREAAKQELERQRRLEWERLRRQELLSQKTREQEDivrlssrkksLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEV 526
Cdd:pfam12128  455 QATATPELLLQLENFDERIERAREEQEAANAEVER----------LQSELRQARKRRDQASEALRQASRRLEERQSALDE 524


                   ....*.
gi 312176405   527 LDKQCD 532
Cdd:pfam12128  525 LELQLF 530
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 380-610 7.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 380 EKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQewkKQLELEKRLEKQRELERQREEERRKEIERREAAKQELERQR 459
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 460 RLEWERLRRQELLSQKTRE-----QEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLE 534
Cdd:COG4942  104 EELAELLRALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312176405 535 IMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQlsntpdsgisllhKKSSEKEELCQRLKEQLDALEKETASK 610
Cdd:COG4942  184 EEERAALEALKAERQKLLARLEKELAELAAELAELQ-------------QEAEELEALIARLEAEAAAAAERTPAA 246
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 368-606 7.88e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.34  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  368 RKANYERGNMELEKRRQVLMEQQQR--EAERKAQ---KEKEEWERKQRELQEQEWKKQlELEKRLEKQrelerqreeerR 442
Cdd:pfam05557 116 LRRQIQRAELELQSTNSELEELQERldLLKAKASeaeQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQ-----------E 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  443 KEIERREAAKQELERqrrlewerlrRQELLSQKTREQEDIVRLSSRKKSLHLELEAVNG------KHQQISGRLQDVQIR 516
Cdd:pfam05557 184 QDSEIVKNSKSELAR----------IPELEKELERLREHNKHLNENIENKLLLKEEVEDlkrkleREEKYREEAATLELE 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  517 KQTQKTEL---EVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIKNMQLSNTP--------DSGISLLHKK 585
Cdd:pfam05557 254 KEKLEQELqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARREleqelaqyLKKIEDLNKK 333

                         250       260
                  ....*....|....*....|.
gi 312176405  586 SSEKEELCQRLKEQLDALEKE 606
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKE 354
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
367-622 8.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 367 KRKANYERGNMELEKR-RQVLME--------QQQREAERKAQKEKEEWERKQRELQEQEwKKQLELEKRLEKqrelerqr 437
Cdd:PRK03918 186 KRTENIEELIKEKEKElEEVLREineisselPELREELEKLEKEVKELEELKEEIEELE-KELESLEGSKRK-------- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 438 eeerrkeierREAAKQELERQRrlewerlrrqELLSQKTREQEDIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVQIRK 517
Cdd:PRK03918 257 ----------LEEKIRELEERI----------EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 518 QTQKTELEVLDKQC-DLEIME--IKQLQQELKEYQNKLIYLVPEKQLLN---------ERIKNMQLSNTPDSGISLLHKK 585
Cdd:PRK03918 317 SRLEEEINGIEERIkELEEKEerLEELKKKLKELEKRLEELEERHELYEeakakkeelERLKKRLTGLTPEKLEKELEEL 396

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 312176405 586 SSEKEELCQRLKEQLDaleketasKLSEMDSFNNQLK 622
Cdd:PRK03918 397 EKAKEEIEEEISKITA--------RIGELKKEIKELK 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 369-533 8.51e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   369 KANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLElekRLEKQRELERQREEERRKEIERR 448
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE---RLEARLERLEDRRERLQQEIEEL 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405   449 EAAKQELERQRRLEWERLRRQELLSQKTREQEDIVRLSSRKKSLHL---ELEAVNGKHQQISGR---LQDVQIRKQT-QK 521
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARldsLERLQENLEGfSE 506

                          170
                   ....*....|..
gi 312176405   522 TELEVLDKQCDL 533
Cdd:TIGR02168  507 GVKALLKNQSGL 518
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 469-622 8.71e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405 469 QELLSQktreqedIVRLSSRKKSLHLELEAVNGKHQQISGRLQDVqirkqtqKTELEVLDKQCDLEIMEIKQLQQELKEY 548
Cdd:COG1579   13 QELDSE-------LDRLEHRLKELPAELAELEDELAALEARLEAA-------KTELEDLEKEIKRLELEIEEVEARIKKY 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312176405 549 QNKLiylvpeKQLLNER-IKNMQLSntpdsgISLLHKKSSEKEELCQRLKEQLDALEKETASKLSEMDSFNNQLK 622
Cdd:COG1579   79 EEQL------GNVRNNKeYEALQKE------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 345-606 9.33e-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: 39.34  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  345 LPSYQKTQEEEPQKKLPVTFEDKRKAnYERgNMELEKRRQvlmEQQQREAERKAQKE-------KEEWERKQRELQEQEW 417
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMA-MER-ERELERIRQ---EERKRELERIRQEEiameisrMRELERLQMERQQKNE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  418 KKQLELE-----KRLEKQRELERQREEERRKE-IERREAAKQE----LERQRRLEWERLRRQELLSQKTREQEDIVRLSS 487
Cdd:pfam17380 393 RVRQELEaarkvKILEEERQRKIQQQKVEMEQiRAEQEEARQRevrrLEEERAREMERVRLEEQERQQQVERLRQQEEER 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  488 RKKSLHLELEAVNGKHQQisgrlqdvQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLNERIK 567
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAE--------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 312176405  568 NMQLSNtpdsgisllHKKSSEKEELCQRLKEQLDALEKE 606
Cdd:pfam17380 545 QQEMEE---------RRRIQEQMRKATEERSRLEAMERE 574
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 349-433 9.59e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.33  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  349 QKTQEEEPQKKLPVTfEDKRKANYERGNME-----LEKRRQVLMEQQQR----EAERKAQKEKEEWERKQRELQEQEWKK 419
Cdd:pfam05672  32 QERLEKEEEERLRKE-ELRRRAEEERARREeearrLEEERRREEEERQRkaeeEAEEREQREQEEQERLQKQKEEAEAKA 110

                          90
                  ....*....|....*
gi 312176405  420 QLELEK-RLEKQREL 433
Cdd:pfam05672 111 REEAERqRQEREKIM 125
PTZ00121 PTZ00121
MAEBL; Provisional
 336-613 9.63e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  336 KQVDSVNGTLPSYQKTQEEEPQKKLpvtfEDKRKANYERGNMELEKRRQVLMEQQQREAERKAQKEKEEWERKQRELQEq 415
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE- 1666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  416 ewKKQLELEKRLEKQRELERQREEERRKEIERREAAKQELERQRRLEWERLRRQELLSQ------------KTREQEDIV 483
Cdd:PTZ00121 1667 --AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeenkikaeeaKKEAEEDKK 1744

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312176405  484 RLSSRKKSlhlELEAVNGKHQQISGRLQDVQIRKQTQKTELEVLDKQCDLEIMEIKQLQQELKEYQNKLIYLVPEKQLLN 563
Cdd:PTZ00121 1745 KAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 312176405  564 ERIKNMQLSNTPDSGISllhkKSSEKEElcqrlkeqLDALEKETASKLSE 613
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADS----KNMQLEE--------ADAFEKHKFNKNNE 1859
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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