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Conserved domains on  [gi|1919270897|ref|NP_001375259|]
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ensconsin isoform 2 [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 organisation of microtubules varies with the cell type and is ...
498-647 2.44e-21

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 91.23  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897 498 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 577
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270897 578 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 647
Cdd:pfam05672  81 AEEEAEEKEQREKEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRLEEIMKRTRKSDAAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
106-181 1.36e-06

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 48.48  E-value: 1.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919270897 106 REIVWLEREERARqhyeKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNR 181
Cdd:pfam05672   1 KPSAGTTDAEEAA----RILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKR 72
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
101-317 7.48e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  101 KQLAAREIV--WLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLE---------EDKERHEAVVRRTM 169
Cdd:PTZ00108  1119 EKLKNTTPKdmWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKkkekkkkksSADKSKKASVVGNS 1198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  170 ERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRR----SVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWES 245
Cdd:PTZ00108  1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQktkpKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRV 1278
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919270897  246 SVVNRLLTPTHSFLARSKSTAALSGEAVIPICPRSASCSPIIMPYK------AAHSRNSMDRPKLFVTPPEGSSRRRI 317
Cdd:PTZ00108  1279 SAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKkksekkTARKKKSKTRVKQASASQSSRLLRRP 1356
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
498-647 2.44e-21

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 91.23  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897 498 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 577
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270897 578 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 647
Cdd:pfam05672  81 AEEEAEEKEQREKEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRLEEIMKRTRKSDAAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
106-181 1.36e-06

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 48.48  E-value: 1.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919270897 106 REIVWLEREERARqhyeKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNR 181
Cdd:pfam05672   1 KPSAGTTDAEEAA----RILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKR 72
PTZ00121 PTZ00121
MAEBL; Provisional
86-179 4.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897   86 DDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVV 165
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
                           90
                   ....*....|....
gi 1919270897  166 rrtmERSQKPKQKH 179
Cdd:PTZ00121  1752 ----DEEEKKKIAH 1761
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
101-317 7.48e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  101 KQLAAREIV--WLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLE---------EDKERHEAVVRRTM 169
Cdd:PTZ00108  1119 EKLKNTTPKdmWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKkkekkkkksSADKSKKASVVGNS 1198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  170 ERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRR----SVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWES 245
Cdd:PTZ00108  1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQktkpKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRV 1278
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919270897  246 SVVNRLLTPTHSFLARSKSTAALSGEAVIPICPRSASCSPIIMPYK------AAHSRNSMDRPKLFVTPPEGSSRRRI 317
Cdd:PTZ00108  1279 SAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKkksekkTARKKKSKTRVKQASASQSSRLLRRP 1356
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
111-174 7.88e-03

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


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 39.16  E-value: 7.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919270897 111 LEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQK 174
Cdd:COG3064    85 EEQVAEELKPKQAAEQERLKQLEKERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKK 148
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
498-647 2.44e-21

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 91.23  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897 498 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 577
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270897 578 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 647
Cdd:pfam05672  81 AEEEAEEKEQREKEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRLEEIMKRTRKSDAAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
106-181 1.36e-06

MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 48.48  E-value: 1.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919270897 106 REIVWLEREERARqhyeKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNR 181
Cdd:pfam05672   1 KPSAGTTDAEEAA----RILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKR 72
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
87-173 5.44e-04

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: 43.57  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  87 DRQRLARERREEREKQLAAREIVWLErEERARQHYEKHLEERKKRLEEqrqkEERRRAAVEEKRRQR-LEEDKERHEAVV 165
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIYE----EERRREAEEERRKQQeMEERRRIQEQMR 559

                  ....*...
gi 1919270897 166 RRTMERSQ 173
Cdd:pfam17380 560 KATEERSR 567
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
112-174 2.39e-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: 39.26  E-value: 2.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919270897 112 EREERARQHYEKHLEERKKRLEEQRQKE-ERRRAAVEEKRRQrlEEDKERHEAVVRRTMERSQK 174
Cdd:pfam15346  74 EEERKKREELERILEENNRKIEEAQRKEaEERLAMLEEQRRM--KEERQRREKEEEEREKREQQ 135
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
104-156 4.37e-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: 4.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1919270897 104 AAREIVWLEREERARQH--YEKHLEERKKRLEEQRQ-KEERRRAAVEEKRRQRLEE 156
Cdd:pfam09756  19 QQREAEEEEREEREKLEekREEEYKEREEREEEAEKeKEEEERKQEEEQERKEQEE 74
PTZ00121 PTZ00121
MAEBL; Provisional
86-179 4.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897   86 DDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVV 165
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
                           90
                   ....*....|....
gi 1919270897  166 rrtmERSQKPKQKH 179
Cdd:PTZ00121  1752 ----DEEEKKKIAH 1761
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
115-178 5.48e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 5.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919270897 115 ERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVR--RTMERSQKPKQK 178
Cdd:PRK00409  540 EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKelRQLQKGGYASVK 605
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
101-317 7.48e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  101 KQLAAREIV--WLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLE---------EDKERHEAVVRRTM 169
Cdd:PTZ00108  1119 EKLKNTTPKdmWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKkkekkkkksSADKSKKASVVGNS 1198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270897  170 ERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRR----SVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWES 245
Cdd:PTZ00108  1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQktkpKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRV 1278
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919270897  246 SVVNRLLTPTHSFLARSKSTAALSGEAVIPICPRSASCSPIIMPYK------AAHSRNSMDRPKLFVTPPEGSSRRRI 317
Cdd:PTZ00108  1279 SAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKkksekkTARKKKSKTRVKQASASQSSRLLRRP 1356
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
111-174 7.88e-03

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


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 39.16  E-value: 7.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1919270897 111 LEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQK 174
Cdd:COG3064    85 EEQVAEELKPKQAAEQERLKQLEKERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKK 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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