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Conserved domains on  [gi|270483747|ref|NP_001161939|]
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MAP7 domain-containing protein 2 isoform 4 [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

 Zoom to residue level

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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 ...
 337-503 6.05e-26

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: 103.97  E-value: 6.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  337 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 416
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  417 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 496
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 270483747  497 KRTRKSD 503
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-102 1.29e-05

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: 48.58  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558

                          90
                  ....*....|....*
gi 270483747   88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 124-255 4.47e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747 124 TSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSYKSSPTRNIEKKKATSTSTSGAGDVGKEALSGGEASLVEK 203
Cdd:PTZ00449 631 KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPET 710

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 270483747 204 VKRGQRTATSLPVVNFGSPlrrcEFSGGIPKRPSSPVISKTATKAYPQSPKT 255
Cdd:PTZ00449 711 PGTPFTTPRPLPPKLPRDE----EFPFEPIGDPDAEQPDDIEFFTPPEEERT 758
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 337-503 6.05e-26

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: 103.97  E-value: 6.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  337 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 416
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  417 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 496
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 270483747  497 KRTRKSD 503
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-102 1.29e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558

                          90
                  ....*....|....*
gi 270483747   88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
PTZ00121 PTZ00121
MAEBL; Provisional
 6-102 3.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 77
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          90       100
                  ....*....|....*....|....*
gi 270483747   78 EEEERLEAMMRRSLERTQQLELKKK 102
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 124-255 4.47e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747 124 TSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSYKSSPTRNIEKKKATSTSTSGAGDVGKEALSGGEASLVEK 203
Cdd:PTZ00449 631 KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPET 710

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 270483747 204 VKRGQRTATSLPVVNFGSPlrrcEFSGGIPKRPSSPVISKTATKAYPQSPKT 255
Cdd:PTZ00449 711 PGTPFTTPRPLPPKLPRDE----EFPFEPIGDPDAEQPDDIEFFTPPEEERT 758
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 9-102 6.17e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQMEERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMM 87
Cdd:TIGR02794  66 EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141

                          90
                  ....*....|....*.
gi 270483747   88 RRSLERTQ-QLELKKK 102
Cdd:TIGR02794 142 RKAKEEAAkQAEEEAK 157
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 9-75 6.99e-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: 39.10  E-value: 6.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270483747   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 75
Cdd:cd16269  197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 337-503 6.05e-26

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: 103.97  E-value: 6.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  337 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 416
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747  417 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 496
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 270483747  497 KRTRKSD 503
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-102 1.29e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558

                          90
                  ....*....|....*
gi 270483747   88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
PTZ00121 PTZ00121
MAEBL; Provisional
 6-102 3.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 77
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          90       100
                  ....*....|....*....|....*
gi 270483747   78 EEEERLEAMMRRSLERTQQLELKKK 102
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 124-255 4.47e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747 124 TSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSYKSSPTRNIEKKKATSTSTSGAGDVGKEALSGGEASLVEK 203
Cdd:PTZ00449 631 KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPET 710

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 270483747 204 VKRGQRTATSLPVVNFGSPlrrcEFSGGIPKRPSSPVISKTATKAYPQSPKT 255
Cdd:PTZ00449 711 PGTPFTTPRPLPPKLPRDE----EFPFEPIGDPDAEQPDDIEFFTPPEEERT 758
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 9-102 6.17e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQMEERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMM 87
Cdd:TIGR02794  66 EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141

                          90
                  ....*....|....*.
gi 270483747   88 RRSLERTQ-QLELKKK 102
Cdd:TIGR02794 142 RKAKEEAAkQAEEEAK 157
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 9-102 6.64e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERREEREkclAAREQQILEKQK------------RARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKL 76
Cdd:pfam17380 386 ERQQKNERVRQELE---AARKVKILEEERqrkiqqqkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462

                          90       100
                  ....*....|....*....|....*.
gi 270483747   77 REEEERLEAMMRRSLERTQQLELKKK 102
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKR 488
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 9-75 6.99e-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: 39.10  E-value: 6.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270483747   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 75
Cdd:cd16269  197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 9-104 8.36e-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: 37.34  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270483747    9 ERQRLAKERRE--EREKCLAAREQQILEKQKRA-RLQYEKQMEERWRKLEE-QRQREDQKRAAVEEKRKQKlrEEEERLE 84
Cdd:pfam15346  46 ARKIMEKQVLEelEREREAELEEERRKEEEERKkREELERILEENNRKIEEaQRKEAEERLAMLEEQRRMK--EERQRRE 123

                          90       100
                  ....*....|....*....|
gi 270483747   85 AMMRRSLERTQQLELKKKYS 104
Cdd:pfam15346 124 KEEEEREKREQQKILNKKNS 143
 
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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