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Conserved domains on  [gi|347968986|ref|XP_001688351|]
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AGAP002984-PA [Anopheles gambiae str. PEST]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-246 3.11e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKE------EQEEHSKSSMEANIR 104
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleeELEELEEELEELEEE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 105 YASLQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRyQQESANDVEHLKAQIVQLKSDKLNLEATLR 184
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELE 424
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347968986 185 RQLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-246 3.11e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKE------EQEEHSKSSMEANIR 104
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleeELEELEEELEELEEE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 105 YASLQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRyQQESANDVEHLKAQIVQLKSDKLNLEATLR 184
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELE 424
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347968986 185 RQLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
45-213 9.24e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   45 EQQQKSVQAQMEVIVDQKLRLENSLESER--------MINEA-----NRKELKQKAKEEQEEHSKSSMEANIRYASLQQQ 111
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQqeinekttEISNTqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  112 CNLVKSQLGDVteecsrsKKQQSEEINSlRLKvSELQGKVQRYQQ------ESANDVEHLKAQIVQLKSDKLNLEA---T 182
Cdd:TIGR04523 290 LNQLKSEISDL-------NNQKEQDWNK-ELK-SELKNQEKKLEEiqnqisQNNKIISQLNEQISQLKKELTNSESensE 360
                         170       180       190
                  ....*....|....*....|....*....|.
gi 347968986  183 LRRQLAEKDHVIEqmrdlatKMEKENAHYLE 213
Cdd:TIGR04523 361 KQRELEEKQNEIE-------KLKKENQSYKQ 384
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
44-240 3.26e-05

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: 47.41  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   44 CEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELK---QKAKEEQEEHSKSSMEANIRYASLQQQCNLVKSQLG 120
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  121 DVT---EECSRSKK-------QQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQIVQLKSDKLNLEATLrrqlaEK 190
Cdd:pfam05483 605 NKNkniEELHQENKalkkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV-----EK 679
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 347968986  191 DHVIEqmrDLATKMEKENAHYLEH--CKLPAEQQpKQHHRYRDVLEalSRDA 240
Cdd:pfam05483 680 AKAIA---DEAVKLQKEIDKRCQHkiAEMVALME-KHKHQYDKIIE--ERDS 725
PTZ00121 PTZ00121
MAEBL; Provisional
42-208 5.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   42 LRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKEEQ---------EEHSKSSMEANIRYASLQQQC 112
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeakkaEEDEKKAAEALKKEAEEAKKA 1704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  113 NLVKSQLGDVTEECSRSKKQqsEEINslRLKVSELQGKVQ---------RYQQESANDVEHLKAQIVQLKSD-KLNLEAT 182
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKA--EEEN--KIKAEEAKKEAEedkkkaeeaKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAV 1780
                         170       180
                  ....*....|....*....|....*.
gi 347968986  183 LRRQLAEKDHVIEQMRDLATKMEKEN 208
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDN 1806
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
92-200 8.35e-04

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 40.84  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  92 EEHSKSSMEANIRYASLQQQCNLVKSqlgdVTEECSRSKKQQSEEINSLRLKVSELQgkVQRYQQESandvEHLKAQIVQ 171
Cdd:cd12926   29 EEYTRTSQELQMKRTAIEAFNETIKI----FEEQGQTQEKCSKEYLERFRREGNEKE--MQRILLNS----ERLKSRIAE 98
                         90       100
                 ....*....|....*....|....*....
gi 347968986 172 LKSDKLNLEATLRRQLAEKDHVIEQMRDL 200
Cdd:cd12926   99 IHESRTKLEQDLRAQASDNREIDKRMNSL 127
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-246 3.11e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKE------EQEEHSKSSMEANIR 104
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleeELEELEEELEELEEE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 105 YASLQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRyQQESANDVEHLKAQIVQLKSDKLNLEATLR 184
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELE 424
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347968986 185 RQLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
45-213 9.24e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   45 EQQQKSVQAQMEVIVDQKLRLENSLESER--------MINEA-----NRKELKQKAKEEQEEHSKSSMEANIRYASLQQQ 111
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQqeinekttEISNTqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  112 CNLVKSQLGDVteecsrsKKQQSEEINSlRLKvSELQGKVQRYQQ------ESANDVEHLKAQIVQLKSDKLNLEA---T 182
Cdd:TIGR04523 290 LNQLKSEISDL-------NNQKEQDWNK-ELK-SELKNQEKKLEEiqnqisQNNKIISQLNEQISQLKKELTNSESensE 360
                         170       180       190
                  ....*....|....*....|....*....|.
gi 347968986  183 LRRQLAEKDHVIEqmrdlatKMEKENAHYLE 213
Cdd:TIGR04523 361 KQRELEEKQNEIE-------KLKKENQSYKQ 384
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
44-240 3.26e-05

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: 47.41  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   44 CEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELK---QKAKEEQEEHSKSSMEANIRYASLQQQCNLVKSQLG 120
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  121 DVT---EECSRSKK-------QQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQIVQLKSDKLNLEATLrrqlaEK 190
Cdd:pfam05483 605 NKNkniEELHQENKalkkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV-----EK 679
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 347968986  191 DHVIEqmrDLATKMEKENAHYLEH--CKLPAEQQpKQHHRYRDVLEalSRDA 240
Cdd:pfam05483 680 AKAIA---DEAVKLQKEIDKRCQHkiAEMVALME-KHKHQYDKIIE--ERDS 725
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-246 5.57e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLGLRCEQQQKSVQAQMEvivdqKLRLENSLESERmINEANRKELKQKAKEEQEEHSKSSMEANIRYAS--- 107
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELE-----ELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEerl 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 108 --LQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRyQQESANDVEHLKAQIVQLKSDKLNLEATLRR 185
Cdd:COG1196  319 eeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEAEEELEELAEELLEALRAAAE 397
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347968986 186 QLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-246 6.35e-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: 46.59  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLES-ERMINEANR-----KELKQKAKEEQEEHSKSSMEANIR 104
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlRKELEELSRqisalRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   105 YASLQQQCNLVKSQLGDVTEECSRSK----------KQQSEEINSLRLKVSELQGKVQRYQQESAN---DVEHLKAQIVQ 171
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEaeieeleaqiEQLKEELKALREALDELRAELTLLNEEAANlreRLESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347968986   172 LKSDKLNLEATLRR---QLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:TIGR02168  836 TERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
49-245 9.54e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    49 KSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKA---KEEQEEHSKSSMEANIRYASLQQQCNLVKSQLGDVTEE 125
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   126 CSRSKKQQS----------EEINSLRLKVSELQGKVQRYQQESA---NDVEHLKAQIVQLKSDKLnleaTLRRQLAEKDH 192
Cdd:TIGR02169  380 FAETRDELKdyrekleklkREINELKRELDRLQEELQRLSEELAdlnAAIAGIEAKINELEEEKE----DKALEIKKQEW 455
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 347968986   193 VIEQMRDLATKMEKenahylEHCKLPAEQQpkqhhRYRDVLEALSRDAAKANA 245
Cdd:TIGR02169  456 KLEQLAADLSKYEQ------ELYDLKEEYD-----RVEKELSKLQRELAEAEA 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-189 1.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  27 FHSSQQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLE-----NSLESERMINEANRKELKQKAKEEQE-EHSKSSME 100
Cdd:COG4717   90 YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqelEALEAELAELPERLEELEERLEELRElEEELEELE 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 101 ANIryASLQQQCNLVKSQLGDVTEEcsrSKKQQSEEINSLRLKVSELQGKVQRYQQEsandVEHLKAQIVQLKSDKLNLE 180
Cdd:COG4717  170 AEL--AELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEE----LEELEEELEQLENELEAAA 240

                 ....*....
gi 347968986 181 atLRRQLAE 189
Cdd:COG4717  241 --LEERLKE 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-246 1.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  10 FFACLALLILMVGFVTMFH-SSQQQLDELRQLGLRCEQQQKSVQAQMEVI-VDQKLRLENSLESERMINEAnrKELKQKA 87
Cdd:COG4717  279 LFLVLGLLALLFLLLAREKaSLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEEL--QELLREA 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  88 KEEQEEhskssmeanIRYASLQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRY-----QQESANDV 162
Cdd:COG4717  357 EELEEE---------LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleELLEALDE 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 163 EHLKAQIVQLKSDKLNLEATLRRQLAEKDHVIEQMRDLATKMEKENAHYlehcklpaeqqpkQHHRYRDVLEALSRDAAK 242
Cdd:COG4717  428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-------------ELEELKAELRELAEEWAA 494

                 ....
gi 347968986 243 ANAL 246
Cdd:COG4717  495 LKLA 498
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-190 1.57e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLglrcEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKEEQEEHSKSSMEaniRYASLQQ 110
Cdd:COG4717   91 AELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE---ELRELEE 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 111 QCNLVKSQLGDVTEECSRSKKQQS----EEINSLRLKVSELQGKVQRYQQEsandVEHLKAQIVQLKSDKLNLEATLRRQ 186
Cdd:COG4717  164 ELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE----LEEAQEELEELEEELEQLENELEAA 239

                 ....
gi 347968986 187 LAEK 190
Cdd:COG4717  240 ALEE 243
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
32-222 3.20e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    32 QQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKEE-----QEEHSKSSMEANIRYA 106
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaQRIHTELQSKMRSRAK 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   107 SLQQQCNLVKSQLGdvTEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQESAnDVEHLKA--QIVQLKSDKLNLEATLR 184
Cdd:TIGR00618  326 LLMKRAAHVKQQSS--IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-LTQHIHTlqQQKTTLTQKLQSLCKEL 402
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 347968986   185 RQLAEKDHVIE----QMRDL------ATKMEKENAHYLEHCKLPAEQQ 222
Cdd:TIGR00618  403 DILQREQATIDtrtsAFRDLqgqlahAKKQQELQQRYAELCAAAITCT 450
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
32-208 3.79e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   32 QQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENS---LESERMINEANRKELKQK--AKE---EQEEHSKSSMEANI 103
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierLKETIIKNNSEIKDLTNQdsVKEliiKNLDNTRESLETQL 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  104 RyaSLQQQCNLVKSQLGDVTEECsrskKQQSEEINSLRLKVSELQGKVQ---RYQQESANDVEHLKA-------QIVQLK 173
Cdd:TIGR04523 471 K--VLSRSINKIKQNLEQKQKEL----KSKEKELKKLNEEKKELEEKVKdltKKISSLKEKIEKLESekkekesKISDLE 544
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 347968986  174 SDKLNLEATLRR-----QLAEKDHVIEQMRDLATKMEKEN 208
Cdd:TIGR04523 545 DELNKDDFELKKenlekEIDEKNKEIEELKQTQKSLKKKQ 584
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
30-209 4.17e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   30 SQQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLEN------SLESERMINEANRKELKQKAKEEQEEhsKSSMEANI 103
Cdd:pfam05557 137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefeiqSQEQDSEIVKNSKSELARIPELEKEL--ERLREHNK 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  104 RYASLQQQCNLVKSQLGDVTEECSRSKKQQsEEINSLRLKVSELQGKVQRY------------------------QQESA 159
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKRKLEREEKYR-EEAATLELEKEKLEQELQSWvklaqdtglnlrspedlsrrieqlQQREI 293
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 347968986  160 NdvehLKAQIVQLKSDKLNLEATLRRQLAEKDHVIEQMRDLATKMEKENA 209
Cdd:pfam05557 294 V----LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
PTZ00121 PTZ00121
MAEBL; Provisional
42-208 5.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   42 LRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKEEQ---------EEHSKSSMEANIRYASLQQQC 112
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeakkaEEDEKKAAEALKKEAEEAKKA 1704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  113 NLVKSQLGDVTEECSRSKKQqsEEINslRLKVSELQGKVQ---------RYQQESANDVEHLKAQIVQLKSD-KLNLEAT 182
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKA--EEEN--KIKAEEAKKEAEedkkkaeeaKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAV 1780
                         170       180
                  ....*....|....*....|....*.
gi 347968986  183 LRRQLAEKDHVIEQMRDLATKMEKEN 208
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDN 1806
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
55-259 6.00e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   55 MEVIVDQKLRLENSL--ESERMINEanRKELKQKA---KEEQEEHSKSSMEANIRYASLQQ----QCNLVKSQLGDV--- 122
Cdd:pfam10174 452 IERLKEQREREDRERleELESLKKE--NKDLKEKVsalQPELTEKESSLIDLKEHASSLASsglkKDSKLKSLEIAVeqk 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  123 TEECSR----SKKQQSEEINS-----LRLKVSELQGKVQRYQQESAN---DVEHLKAQIVQLKSDKL-------NLEATL 183
Cdd:pfam10174 530 KEECSKlenqLKKAHNAEEAVrtnpeINDRIRLLEQEVARYKEESGKaqaEVERLLGILREVENEKNdkdkkiaELESLT 609
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347968986  184 RRQLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYR--DVLEALSRDAAKANALPAHSFNEQLSVSE 259
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQleELMGALEKTRQELDATKARLSSTQQSLAE 687
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
92-200 8.35e-04

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 40.84  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  92 EEHSKSSMEANIRYASLQQQCNLVKSqlgdVTEECSRSKKQQSEEINSLRLKVSELQgkVQRYQQESandvEHLKAQIVQ 171
Cdd:cd12926   29 EEYTRTSQELQMKRTAIEAFNETIKI----FEEQGQTQEKCSKEYLERFRREGNEKE--MQRILLNS----ERLKSRIAE 98
                         90       100
                 ....*....|....*....|....*....
gi 347968986 172 LKSDKLNLEATLRRQLAEKDHVIEQMRDL 200
Cdd:cd12926   99 IHESRTKLEQDLRAQASDNREIDKRMNSL 127
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
49-200 9.30e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   49 KSVQAQMEVIVDQKLRLENSL-ESERMINEANRkELKQKAKEEQEEHSKSSmeaniryaSLQQQCNLVKSQLGDVTEEcs 127
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQIsQNNKIISQLNE-QISQLKKELTNSESENS--------EKQRELEEKQNEIEKLKKE-- 378
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347968986  128 rsKKQQSEEINSLRLKVSELQGKVQRYQQESANdvehLKAQIVQLKSDKLNLEATLRRQLAEKDHVIEQMRDL 200
Cdd:TIGR04523 379 --NQSYKQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
31-205 9.74e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    31 QQQLDELR----QLGLRCEQQQKSVQAQMEVIVD-QKLRLENSLESERMINEANRKELKQKAKEE-----QEEHSKSSME 100
Cdd:TIGR00606  863 KSKTNELKseklQIGTNLQRRQQFEEQLVELSTEvQSLIREIKDAKEQDSPLETFLEKDQQEKEElisskETSNKKAQDK 942
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   101 ANIRYASLQQQCNLVKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQE-----SANDVEHLKAQIVQlksD 175
Cdd:TIGR00606  943 VNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDmrlmrQDIDTQKIQERWLQ---D 1019
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 347968986   176 KLNLE------ATLRRQLAEKDHVIEQMRDLATKME 205
Cdd:TIGR00606 1020 NLTLRkrenelKEVEEELKQHLKEMGQMQVLQMKQE 1055
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-238 1.06e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    80 RKELKQKAKEEQEEHSKSSMEANiRYASLQQQCNLVKSQLGDVTEECSRSKKQQS---EEINSLRLKVSELQGKVQRYQ- 155
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQeleEKLEELRLEVSELEEEIEELQk 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   156 --QESANDVEHLKAQIVQLKSDKLNLEATLRRQLAEKDHViEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVL 233
Cdd:TIGR02168  289 elYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                   ....*
gi 347968986   234 EALSR 238
Cdd:TIGR02168  368 EELES 372
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
87-239 1.48e-03

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: 42.12  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   87 AKEEQEEHSKSSMEA-NIRYASLQQQCNLVKSQLGDVTEECSrskkQQSEEINSLR-------LKVSELQGKVQRYQQ-- 156
Cdd:pfam10174 335 AKEQRAAILQTEVDAlRLRLEEKESFLNKKTKQLQDLTEEKS----TLAGEIRDLKdmldvkeRKINVLQKKIENLQEql 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  157 -ESANDVEHLKAQIVQLKSDKLNLE---ATLRRQLAEKDHVIEQMRDLATKMEKENAHYLEHCKlpaeqqpKQHHRYRDV 232
Cdd:pfam10174 411 rDKDKQLAGLKERVKSLQTDSSNTDtalTTLEEALSEKERIIERLKEQREREDRERLEELESLK-------KENKDLKEK 483

                  ....*..
gi 347968986  233 LEALSRD 239
Cdd:pfam10174 484 VSALQPE 490
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
49-246 2.13e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   49 KSVQAQMEVIVDQKLRLENSLESERMINEANR--KELKQKAKEEQEEhsKSSMEANIRYASLQQQCNLVKSQLgdvtEEC 126
Cdd:PRK10929   48 EALQSALNWLEERKGSLERAKQYQQVIDNFPKlsAELRQQLNNERDE--PRSVPPNMSTDALEQEILQVSSQL----LEK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  127 SRSKKQQSE---EINSLRLKVSELQGKVQRYQQESANDVEHL--------KAQIVQLKS---------DKLNLE------ 180
Cdd:PRK10929  122 SRQAQQEQDrarEISDSLSQLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAesaalkalvDELELAqlsann 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  181 ----ATLRRQLAEK-----DHVIEQMRD-LATKMEKENAHYLEHCKLPAEQQ---PK----QHHRYRDVLEALSRDAAKA 243
Cdd:PRK10929  202 rqelARLRSELAKKrsqqlDAYLQALRNqLNSQRQREAERALESTELLAEQSgdlPKsivaQFKINRELSQALNQQAQRM 281

                  ...
gi 347968986  244 NAL 246
Cdd:PRK10929  282 DLI 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-238 2.58e-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: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    30 SQQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERmiNEANRKELKQKAKEEQEEHSKSSMEAniryasLQ 109
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR--ERLANLERQLEELEAQLEELESKLDE------LA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   110 QQCNLVKSQLGDVTEECsrskKQQSEEINSLRLKVSELQGKVQRYQQES---ANDVEHLKAQIVQLKSDKLNLEATLRRQ 186
Cdd:TIGR02168  337 EELAELEEKLEELKEEL----ESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLNNEIERLEARLERL 412
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 347968986   187 LAEKDHVIEQMRDLATKMEKENAHYL-EHCKLPAEQQPKQHHRYRDVLEALSR 238
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEE 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
61-206 2.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  61 QKLRLENSLESERMINEANRKELKqKAKEEQEEHSKSSMEANIRYASLQQQCNLVKSQLGDvTEECSRSKKQQSEEINSL 140
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLE-KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEK 281
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347968986 141 RLKVSELQGKVQRYqqesandvEHLKAQIVQLKSDKLNLEATLRRQLAEKDHVIEQMRDLATKMEK 206
Cdd:PRK03918 282 VKELKELKEKAEEY--------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-246 2.84e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQ--LGLRCEQQQKSVQAQMEVIVDQKLRLEnSLESERMINEANRKELKQKAKEEQEEhskssmeanirYASL 108
Cdd:COG1196  219 KEELKELEAelLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEAELEELRLELEELELE-----------LEEA 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 109 QQQCNLVKSQLGDVTEECSRSKKQQ---SEEINSLRLKVSELQGKVQRYQQEsandVEHLKAQIVQLKSDKLNLEATLRR 185
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAE 362
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347968986 186 QLAEKDHVIEQMRDLATKMEKENAHYLEHCKLPAEQQPKQHHRYRDVLEALSRDAAKANAL 246
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
7-209 3.20e-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: 40.52  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   7 RSRFFACLALLILMVGFVTMFHSSQQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSL-ESERMINEAN------ 79
Cdd:COG4942    2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaALARRIRALEqelaal 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  80 RKELKQKAKEEQE-----EHSKSSMEANIRYASLQQQCNLVKSQLG-----------DVTEECSRSKKQQSEEINSLRLK 143
Cdd:COG4942   82 EAELAELEKEIAElraelEAQKEELAELLRALYRLGRQPPLALLLSpedfldavrrlQYLKYLAPARREQAEELRADLAE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347968986 144 VSELQGKVQRYQQESANDVEHLKAQIVQLKSDKLNLEATL----------RRQLAEKDHVIEQMRDLATKMEKENA 209
Cdd:COG4942  162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLarlekelaelAAELAELQQEAEELEALIARLEAEAA 237
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
31-199 3.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQkAKEEQEEHSKSSMEANIRYASLQQ 110
Cdd:COG4372   51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQ 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986 111 QCNLVKSQLgdvtEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQIVQLKSDKLNLEATLRRQLAEK 190
Cdd:COG4372  130 QRKQLEAQI----AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205

                 ....*....
gi 347968986 191 DHVIEQMRD 199
Cdd:COG4372  206 EKLIESLPR 214
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
88-185 3.85e-03

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.89  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   88 KEEQEEHSKSSMEANIRYASLQQQCnLVKSQLGDVTEECSRSKKQQSE----EINSLRLKVSELQGKVQRYQQESANDVE 163
Cdd:pfam07111 323 KAQDLEHRDSVKQLRGQVAELQEQV-TSQSQEQAILQRALQDKAAEVEvermSAKGLQMELSRAQEARRRQQQQTASAEE 401
                          90       100
                  ....*....|....*....|..
gi 347968986  164 HLKAQIVQLKSDKLNLEATLRR 185
Cdd:pfam07111 402 QLKFVVNAMSSTQIWLETTMTR 423
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
45-200 3.87e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   45 EQQQKSVQAQMEVIVD---QKLRLENSLESERMINEANRkelkQKAKEEQEEHSKSsmeaniryASLQQQCNLVKSQLGD 121
Cdd:pfam05667 254 EQLRSAALAGTEATSGasrSAQDLAELLSSFSGSSTTDT----GLTKGSRFTHTEK--------LQFTNEAPAATSSPPT 321
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347968986  122 VTEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQEsandVEHLKAQIVQLKSDKLNLEATlRRQLAEKDHVIEQMRDL 200
Cdd:pfam05667 322 KVETEEELQQQREEELEELQEQLEDLESSIQELEKE----IKKLESSIKQVEEELEELKEQ-NEELEKQYKVKKKTLDL 395
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
31-191 3.95e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.43  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLE--NSLESERMIN-EANRKELkQKAKEEQEEHSKSSMEANIRYAS 107
Cdd:pfam15742 171 KQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLEmtNSQQQLRIQQqEAQLKQL-ENEKRKSDEHLKSNQELSEKLSS 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  108 LQQQCNLVKsqlgdvtEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQIVQLKSdklnlEATLRRQL 187
Cdd:pfam15742 250 LQQEKEALQ-------EELQQVLKQLDVHVRKYNEKHHHHKAKLRRAKDRLVHEVEQRDERIKQLEN-----EIGILQQQ 317

                  ....
gi 347968986  188 AEKD 191
Cdd:pfam15742 318 SEKE 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-181 5.37e-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: 40.43  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986    31 QQQLDELRQLGLRCEQQQKSVQAQMEVIVDQKLRLENSLESERMINEANRKELKQKAKEEQ----EEHSKSSMEANIRYA 106
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaelEELEEELEELQEELE 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   107 SLQQQCNLVKSQLgdvtEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQ-----IVQLKSDKLNLEA 181
Cdd:TIGR02168  458 RLEEALEELREEL----EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgILGVLSELISVDE 533
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
45-210 8.76e-03

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.


Pssm-ID: 462752 [Multi-domain]  Cd Length: 307  Bit Score: 39.18  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986   45 EQQQKSVQAQMEVIVDQ--KLRLENSLESERMINE-ANRKELKQKAKEEQEEHS-------KSSMEANIRYASLQQQCNL 114
Cdd:pfam09311   8 EKQLQAIQEQEAETRDQvkKLQEMLRQANDQLEKTmKDKKELEDKMNQLSEETSnqvstlaKRNQKSETLLDELQQAFSQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347968986  115 VKSQLGDVTEECSRSKKQQSEEINSLRLKVSELQGKVQRYQQESANDVEHLKAQIVQLKSDKLNLEATLRRQLAEKDHVI 194
Cdd:pfam09311  88 AKRNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHME 167
                         170       180
                  ....*....|....*....|
gi 347968986  195 EQMRD----LATKMEKENAH 210
Cdd:pfam09311 168 EKLKAeilfLKEQIQAEQCL 187
 
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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