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Conserved domains on  [gi|2462628927|ref|XP_054182775|]
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MAP7 domain-containing protein 2 isoform X3 [Homo sapiens]

Protein Classification

MAP7 domain-containing protein( domain architecture ID 12064852)

MAP7 domain-containing protein such as MAP7D1 (microtubule-associated protein 7 domain containing 1) identified as a novel substrate of doublecortin-like kinase 1 (DCLK1)

Gene Ontology:  GO:0005737

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 422-588 5.42e-27

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


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 107.43  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 422 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 501
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 502 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 581
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 2462628927 582 KRTRKSD 588
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-146 6.84e-06

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462628927 112 VEEKRKQKLREEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 167-388 6.66e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  167 TPPPPLGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPpmnkrlSSSTVAIsysPDRVFHVCPRLAPLGPLN 246
Cdd:PHA03247  2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP------ADPPAAV---LAPAAALPPAASPAGPLP 2829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  247 PSYKSSPTRNIEKKKATSTSTSGAGDVGKealsggeaslvekvkrgqrtatslpvvnfGSPLRRcefsggipKRPSSPVI 326
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----------------------------GGDVRR--------RPPSRSPA 2872

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628927  327 SKTATKAYPQSPKTTKPPYPGSPVKYRLPalsgQDMPKRKAEKEKSNKEREGTLAQQAAGPQ 388
Cdd:PHA03247  2873 AKPAAPARPPVRRLARPAVSRSTESFALP----PDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 422-588 5.42e-27

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 107.43  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 422 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 501
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 502 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 581
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 2462628927 582 KRTRKSD 588
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-146 6.84e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462628927 112 VEEKRKQKLREEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 13-146 3.62e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  13 RPEGTARGTSLPGKIAEPGAVrTSQPNYRPQGMEGFLKSdERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQME 92
Cdd:TIGR02794  28 KPEPGGGAEIIQAVLVDPGAV-AQQANRIQQQKKPAAKK-EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462628927  93 ERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMMRRSLERTQ-QLELKKK 146
Cdd:TIGR02794 102 KAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkQAEEEAK 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 167-388 6.66e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  167 TPPPPLGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPpmnkrlSSSTVAIsysPDRVFHVCPRLAPLGPLN 246
Cdd:PHA03247  2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP------ADPPAAV---LAPAAALPPAASPAGPLP 2829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  247 PSYKSSPTRNIEKKKATSTSTSGAGDVGKealsggeaslvekvkrgqrtatslpvvnfGSPLRRcefsggipKRPSSPVI 326
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----------------------------GGDVRR--------RPPSRSPA 2872

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628927  327 SKTATKAYPQSPKTTKPPYPGSPVKYRLPalsgQDMPKRKAEKEKSNKEREGTLAQQAAGPQ 388
Cdd:PHA03247  2873 AKPAAPARPPVRRLARPAVSRSTESFALP----PDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 1.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 121
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                           90       100
                   ....*....|....*....|....*
gi 2462628927  122 EEEERLEAMMRRSLERTQQLELKKK 146
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 53-119 3.77e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628927  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 119
Cdd:cd16269   197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-142 9.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQyekQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEAMMR 132
Cdd:COG4717   109 AELEELREELEKLEKLLQLLPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                          90
                  ....*....|
gi 2462628927 133 RSLERTQQLE 142
Cdd:COG4717   186 LSLATEEELQ 195
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 422-588 5.42e-27

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 107.43  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 422 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 501
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 502 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 581
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 2462628927 582 KRTRKSD 588
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-146 6.84e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462628927 112 VEEKRKQKLREEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 13-146 3.62e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  13 RPEGTARGTSLPGKIAEPGAVrTSQPNYRPQGMEGFLKSdERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQME 92
Cdd:TIGR02794  28 KPEPGGGAEIIQAVLVDPGAV-AQQANRIQQQKKPAAKK-EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462628927  93 ERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMMRRSLERTQ-QLELKKK 146
Cdd:TIGR02794 102 KAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkQAEEEAK 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 167-388 6.66e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  167 TPPPPLGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPpmnkrlSSSTVAIsysPDRVFHVCPRLAPLGPLN 246
Cdd:PHA03247  2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP------ADPPAAV---LAPAAALPPAASPAGPLP 2829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  247 PSYKSSPTRNIEKKKATSTSTSGAGDVGKealsggeaslvekvkrgqrtatslpvvnfGSPLRRcefsggipKRPSSPVI 326
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----------------------------GGDVRR--------RPPSRSPA 2872

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628927  327 SKTATKAYPQSPKTTKPPYPGSPVKYRLPalsgQDMPKRKAEKEKSNKEREGTLAQQAAGPQ 388
Cdd:PHA03247  2873 AKPAAPARPPVRRLARPAVSRSTESFALP----PDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 163-345 7.57e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 163 ESENTPPPPLGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPPMNKRLSSSTVAISYSPDRVFHVCPRlaPL 242
Cdd:PTZ00449  503 DSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKK--PE 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927 243 GPLNPSYKSSPtrniEKKKATSTSTSGAGDVGKEALSGGEASLVEKVKRGQRTATS--LPVvnfgSPLRRCEfsggiPKR 320
Cdd:PTZ00449  581 FPKDPKHPKDP----EEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSpkRPP----PPQRPSS-----PER 647

                         170       180
                  ....*....|....*....|....*
gi 2462628927 321 PSSPVISKTatkayPQSPKTTKPPY 345
Cdd:PTZ00449  648 PEGPKIIKS-----PKPPKSPKPPF 667
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 53-148 1.14e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.03  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKERRE--EREKCLAAREQQILEKQKRA-RLQYEKQMEERWRKLEE-QRQREDQKRAAVEEKRKQKlrEEEERLE 128
Cdd:pfam15346  46 ARKIMEKQVLEelEREREAELEEERRKEEEERKkREELERILEENNRKIEEaQRKEAEERLAMLEEQRRMK--EERQRRE 123

                          90       100
                  ....*....|....*....|
gi 2462628927 129 AMMRRSLERTQQLELKKKYS 148
Cdd:pfam15346 124 KEEEEREKREQQKILNKKNS 143
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 1.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 121
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                           90       100
                   ....*....|....*....|....*
gi 2462628927  122 EEEERLEAMMRRSLERTQQLELKKK 146
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 19-119 2.91e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  19 RGTSLPGKIAEPGAVRTSQPNYRPQGMEGFLKSDERQ--RLAKERREEREKCLAAREQQilEKQKRARLQYEKQMEERWR 96
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmeRVRLEEQERQQQVERLRQQE--EERKRKKLELEKEKRDRKR 488

                          90       100
                  ....*....|....*....|....*...
gi 2462628927  97 KLEEQR-----QREDQKRAAVEEKRKQK 119
Cdd:pfam17380 489 AEEQRRkilekELEERKQAMIEEERKRK 516
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 52-119 3.41e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 3.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462628927  52 DERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 119
Cdd:pfam13868  58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 53-119 3.77e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 3.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628927  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 119
Cdd:cd16269   197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 50-119 4.43e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.87  E-value: 4.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  50 KSDERQRLAKERREEREKclaarEQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 119
Cdd:pfam09756   6 KKRAKLELKEAKRQQREA-----EEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERK 70
rne PRK10811
ribonuclease E; Reviewed
 53-195 4.55e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   53 ERQRlaKERREEREKCLAAREQQILEKQKRARLQYEKQMEERwrkLEEQRQREDQKRAA--------VEEKRKQKLREEE 124
Cdd:PRK10811   637 EENR--RNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPR---RERQRRRNDEKRQAqqeakalnVEEQSVQETEQEE 711

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628927  125 ERLEAMMRRsleRTQQLELKKKY-SWGAPLAIGPGGHDGESENT-----PPPPLGLAASTLPPDAGTTAAAAESTNA 195
Cdd:PRK10811   712 RVQQVQPRR---KQRQLNQKVRIeQSVAEEAVAPVVEETVAAEPvvqevPAPRTELVKVPLPVVAQTAPEQDEENNA 785
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 53-146 5.24e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKERREEREkclAAREQQILEKQK------------RARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKL 120
Cdd:pfam17380 386 ERQQKNERVRQELE---AARKVKILEEERqrkiqqqkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462

                          90       100
                  ....*....|....*....|....*.
gi 2462628927 121 REEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKR 488
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 53-145 5.27e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQM---EERWRKL----EEQRQREDQKRAAVEEKRKQKLREEEE 125
Cdd:pfam15558  51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQViekESRWREQaedqENQRQEKLERARQEAEQRKQCQEQRLK 130

                          90       100
                  ....*....|....*....|
gi 2462628927 126 RLEAMMRRSLERTQQLELKK 145
Cdd:pfam15558 131 EKEEELQALREQNSLQLQER 150
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 54-107 5.38e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.87  E-value: 5.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462628927  54 RQRLAKER-REEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQ 107
Cdd:pfam09756  19 QQREAEEEeREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQE 73
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 48-118 6.44e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 39.63  E-value: 6.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462628927  48 FLKSDER-QRLAKER-REEREKclAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 118
Cdd:pfam15558 206 LQRSQENyEQLVEERhRELREK--AQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQVAHKTVQ 276
PTZ00121 PTZ00121
MAEBL; Provisional
 50-118 6.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   50 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 118
Cdd:PTZ00121  1669 KAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 7.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEA 129
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530

                           90
                   ....*....|....*..
gi 2462628927  130 MMRRSLERTQQLELKKK 146
Cdd:PTZ00121  1531 EEAKKADEAKKAEEKKK 1547
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 53-140 7.30e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKER--REEREKclaaREQQILEKQKRARLQyEKQMEERWRKLEEQRQREDQKRAAvEEKRKQKLREEEERLEAM 130
Cdd:pfam05672  18 EKRRQAREQreREEQER----LEKEEEERLRKEELR-RRAEEERARREEEARRLEEERRRE-EEERQRKAEEEAEEREQR 91

                          90
                  ....*....|
gi 2462628927 131 MRRSLERTQQ 140
Cdd:pfam05672  92 EQEEQERLQK 101
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 8.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927   50 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLE 128
Cdd:PTZ00121  1641 KEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720

                           90
                   ....*....|....*...
gi 2462628927  129 AMMRRSLERTQQLELKKK 146
Cdd:PTZ00121  1721 LKKAEEENKIKAEEAKKE 1738
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-142 9.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQyekQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEAMMR 132
Cdd:COG4717   109 AELEELREELEKLEKLLQLLPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185

                          90
                  ....*....|
gi 2462628927 133 RSLERTQQLE 142
Cdd:COG4717   186 LSLATEEELQ 195
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 52-118 9.63e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 9.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628927  52 DERQRLAKERREEREKCLA---AREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 118
Cdd:pfam13868  40 EEERRLDEMMEEERERALEeeeEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
 
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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