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Conserved domains on  [gi|578828936|ref|XP_006721238|]
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dynein regulatory complex subunit 4 isoform X1 [Homo sapiens]

Protein Classification

GAS domain-containing protein( domain architecture ID 12155935)

GAS (growth-arrest specific micro-tubule binding) domain-containing protein similar to Homo sapiens dynein regulatory complex subunit 4, also known as GAS-8/GAS-11, which is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes

Gene Ontology:  GO:0031514|GO:0048870

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
138-337 5.65e-78

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 239.04  E-value: 5.65e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  138 TLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANY 217
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  218 ERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEK 297
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578828936  298 KEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDL 337
Cdd:pfam13851 161 KEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
Mitofilin super family cl26613
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
42-127 3.93e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


The actual alignment was detected with superfamily member pfam09731:

Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 39.35  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   42 KLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKmlrdeLDLRR 121
Cdd:pfam09731 298 QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLR-----TELER 372

                  ....*.
gi 578828936  122 KTELHE 127
Cdd:pfam09731 373 QAEAHE 378
 
Name Accession Description Interval E-value
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
138-337 5.65e-78

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 239.04  E-value: 5.65e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  138 TLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANY 217
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  218 ERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEK 297
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578828936  298 KEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDL 337
Cdd:pfam13851 161 KEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-357 3.28e-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: 49.28  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    80 LRLKHTEE----ITRMRNDFERQVR--EIEAKYDKKMKMLRDELD-------LRRKTELHEVEERKNGQIHTLMQRHEEA 146
Cdd:TIGR02168  179 RKLERTREnldrLEDILNELERQLKslERQAEKAERYKELKAELRelelallVLRLEELREELEELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   147 FTDIKNYYNDITLNNLAlINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILlc 226
Cdd:TIGR02168  259 TAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   227 tKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQktgFKNLVLERKLQALSAAvekKEVQFNEVL 306
Cdd:TIGR02168  336 -AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKVAQLELQIASLN---NEIERLEAR 408
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578828936   307 AASnLDPAALTLVSRKLEDVLESKNSTIKDLQYELAQVCKAHNDLLRTYEA 357
Cdd:TIGR02168  409 LER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
163-343 9.74e-05

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: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 163 ALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILlctKARLKVREKELKDLQ 242
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 243 WEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAALTLVSRK 322
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180
                 ....*....|....*....|.
gi 578828936 323 LEDVLESKNSTIKDLQYELAQ 343
Cdd:COG1196  403 EELEEAEEALLERLERLEEEL 423
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
42-127 3.93e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 39.35  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   42 KLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKmlrdeLDLRR 121
Cdd:pfam09731 298 QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLR-----TELER 372

                  ....*.
gi 578828936  122 KTELHE 127
Cdd:pfam09731 373 QAEAHE 378
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
111-315 9.18e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 38.01  E-value: 9.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 111 KMLRDELDLRRKTELHEVEERKNGQIHTLMQRHE-----EAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLERE 185
Cdd:PTZ00436  43 KLIKDGLIIRKPVKVHSRSRWRHMKEAKSMGRHEgagrrEGTREARMPSKELWMRRLRILRRLLRKYREEKKIDRHIYRE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 186 M-----AEVSGQNKRLADPLQKAREEMSEmQKQLANyerdkqillctkarlKVREKELKDLQWEHEVLEQRFTKVQQERD 260
Cdd:PTZ00436 123 LyvkakGNVFRNKRNLMEHIHKVKNEKKK-ERQLAE---------------QLAAKRLKDEQHRHKARKQELRKREKDRE 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578828936 261 ELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAA 315
Cdd:PTZ00436 187 RARREDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAA 241
 
Name Accession Description Interval E-value
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
138-337 5.65e-78

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 239.04  E-value: 5.65e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  138 TLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANY 217
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  218 ERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEK 297
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578828936  298 KEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDL 337
Cdd:pfam13851 161 KEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-357 3.28e-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: 49.28  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    80 LRLKHTEE----ITRMRNDFERQVR--EIEAKYDKKMKMLRDELD-------LRRKTELHEVEERKNGQIHTLMQRHEEA 146
Cdd:TIGR02168  179 RKLERTREnldrLEDILNELERQLKslERQAEKAERYKELKAELRelelallVLRLEELREELEELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   147 FTDIKNYYNDITLNNLAlINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILlc 226
Cdd:TIGR02168  259 TAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-- 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   227 tKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQktgFKNLVLERKLQALSAAvekKEVQFNEVL 306
Cdd:TIGR02168  336 -AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKVAQLELQIASLN---NEIERLEAR 408
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578828936   307 AASnLDPAALTLVSRKLEDVLESKNSTIKDLQYELAQVCKAHNDLLRTYEA 357
Cdd:TIGR02168  409 LER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
60-337 2.35e-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: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    60 RALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAkydkKMKMLRDELDLRRKtELHEVEERKNGQIHTL 139
Cdd:TIGR02168  216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRL-EVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   140 mqrheeaftdiknyynditLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLanyER 219
Cdd:TIGR02168  291 -------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL---EE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   220 DKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQktgfknlvLERKLQALSAAVEKKE 299
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER--------LEARLERLEDRRERLQ 420
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 578828936   300 VQFNEVLaaSNLDPAALTLVSRKLEDVLESKNSTIKDL 337
Cdd:TIGR02168  421 QEIEELL--KKLEEAELKELQAELEELEEELEELQEEL 456
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
163-343 9.74e-05

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: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 163 ALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILlctKARLKVREKELKDLQ 242
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 243 WEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAALTLVSRK 322
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180
                 ....*....|....*....|.
gi 578828936 323 LEDVLESKNSTIKDLQYELAQ 343
Cdd:COG1196  403 EELEEAEEALLERLERLEEEL 423
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-296 5.64e-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: 42.36  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    43 LAQKEHRIQEsvLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLR----DELD 118
Cdd:TIGR02169  253 LEKLTEEISE--LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEErlakLEAE 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   119 LRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDItLNNLALINS----LKEQMEDMRKKEDHLEREMAEVSGQNK 194
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL-RAELEEVDKefaeTRDELKDYREKLEKLKREINELKRELD 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   195 RLADPLQKAREEMSEMQKQLANYERDKQILlctKARLKVREKELKDLQWEHEVLEQRFTKVQQErdelYRKFTAAIQEVQ 274
Cdd:TIGR02169  410 RLQEELQRLSEELADLNAAIAGIEAKINEL---EEEKEDKALEIKKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVE 482
                          250       260
                   ....*....|....*....|..
gi 578828936   275 QKTGFKNLVLERKLQALSAAVE 296
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEE 504
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
108-314 8.35e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 108 KKMKMLRDELDLRRKT--ELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLNNlALINSLKEQMEDMRKKEDHLERE 185
Cdd:COG4942   27 AELEQLQQEIAELEKElaALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-AELAELEKEIAELRAELEAQKEE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 186 MAEV------SGQNKRLA------DPLQKAREEM------SEMQKQLANYERDKQILLCTKARLKVREKELKDLQWEHEV 247
Cdd:COG4942  106 LAELlralyrLGRQPPLAlllspeDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828936 248 LEQRFTKVQQERDELYRKFTAAIQEVQQKTGfKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPA 314
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
42-127 3.93e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 39.35  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   42 KLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKmlrdeLDLRR 121
Cdd:pfam09731 298 QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLR-----TELER 372

                  ....*.
gi 578828936  122 KTELHE 127
Cdd:pfam09731 373 QAEAHE 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-262 4.42e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   81 RLKHTEEITRMRNDFERQVREIEAKyDKKMKMLRDELDLRRKTELHEVEERKNGQIHTLM-------QRHEEAFTDIKNY 153
Cdd:COG4913   250 QIELLEPIRELAERYAAARERLAEL-EYLRAALRLWFAQRRLELLEAELEELRAELARLEaelerleARLDALREELDEL 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  154 YNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANyerdkqillcTKARLKV 233
Cdd:COG4913   329 EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEE 398
                         170       180       190
                  ....*....|....*....|....*....|...
gi 578828936  234 REKELKDLQWEHEV----LEQRFTKVQQERDEL 262
Cdd:COG4913   399 ELEALEEALAEAEAalrdLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-296 7.16e-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: 38.50  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936     1 MEEAEER-HQVEIKVykQKVKHLLYEHQNNLTEMKAEGTvvmKLAQKEHRIQESVLRKDMRALKVELKEQELASEVV-VK 78
Cdd:TIGR02168  686 IEELEEKiAELEKAL--AELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeLE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    79 NLRLKHTEEITRMRNDFERQVREIEaKYDKKMKMLRDELDL--RRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYND 156
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKAlrEALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   157 ITL------NNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILlctKAR 230
Cdd:TIGR02168  840 LEDleeqieELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL---RRE 916
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828936   231 LKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVE 296
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
111-315 9.18e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 38.01  E-value: 9.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 111 KMLRDELDLRRKTELHEVEERKNGQIHTLMQRHE-----EAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLERE 185
Cdd:PTZ00436  43 KLIKDGLIIRKPVKVHSRSRWRHMKEAKSMGRHEgagrrEGTREARMPSKELWMRRLRILRRLLRKYREEKKIDRHIYRE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936 186 M-----AEVSGQNKRLADPLQKAREEMSEmQKQLANyerdkqillctkarlKVREKELKDLQWEHEVLEQRFTKVQQERD 260
Cdd:PTZ00436 123 LyvkakGNVFRNKRNLMEHIHKVKNEKKK-ERQLAE---------------QLAAKRLKDEQHRHKARKQELRKREKDRE 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578828936 261 ELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAA 315
Cdd:PTZ00436 187 RARREDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAA 241
PTZ00121 PTZ00121
MAEBL; Provisional
1-328 9.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936    1 MEEAEERHQVEIKVYKQKVKHLLYEHQNNLTEMKAEgtvvmklaqKEHRIQESVLRKDMRALKVELKEQELASEVVVKNL 80
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936   81 RLKHTEEITRMRNDFERQVREIEAKYDKKMKmlRDELDLRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLN 160
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  161 NLALINSLKEQMEDMRKKEDHLEREmaEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQillcTKARLKVREKELKD 240
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE----DEKRRMEVDKKIKD 1802
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  241 LQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKtgfKNLVLERklqalSAAVEKKEVQFNEVLAASNLDPAALTLVS 320
Cdd:PTZ00121 1803 IFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADS---KNMQLEE-----ADAFEKHKFNKNNENGEDGNKEADFNKEK 1874

                  ....*...
gi 578828936  321 RKLEDVLE 328
Cdd:PTZ00121 1875 DLKEDDEE 1882
PRK12704 PRK12704
phosphodiesterase; Provisional
66-213 9.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 9.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828936  66 LKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLRD-ELDLRRKTELHEVEERK-NGQIHTLMQRH 143
Cdd:PRK12704  44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKREEElEKKEKELEQKQ 123
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828936 144 EEaftdiknyynditlnnlalinsLKEQMEDMRKKEDHLEREMAEVSGQNK-----RLADPL-QKAREEMSEMQKQ 213
Cdd:PRK12704 124 QE----------------------LEKKEEELEELIEEQLQELERISGLTAeeakeILLEKVeEEARHEAAVLIKE 177
 
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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