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Conserved domains on  [gi|310750354|ref|NP_001185540|]
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ensconsin 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

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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 ...
453-602 2.74e-20

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: 88.15  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  453 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 532
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750354  533 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 602
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 7.35e-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: 46.55  E-value: 7.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354  106 REIVWLEREERARqhyeKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNR 181
Cdd:pfam05672   1 KPSAGTTDAEEAA----RILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKR 72
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
127-406 9.12e-04

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: 42.73  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  127 ERKKRLEEQRQKEERRRAAVEEK------RR--QRLEEDKERHEAVVRRTMERSQKPKQKHNRWSwgGSLHGSPSIHSAA 198
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmwLEdlDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKA--SKLRKPKLKKKEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  199 RRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAAScspiiMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTAS 278
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKS-----NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSS 1254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  279 YKKERERENVLFLTSGTRRAVSPSNPKARQPARsrlwlPSKSLPHLP-GTPRPTSSlppgSVKAAPAQVRPPSPGNIRPV 357
Cdd:PTZ00108 1255 EDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPP-----PSKRPDGESnGGSKPSSP----TKKKVKKRLEGSLAALKKKK 1325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 310750354  358 KREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPE 406
Cdd:PTZ00108 1326 KSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVD 1374
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
453-602 2.74e-20

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: 88.15  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  453 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 532
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750354  533 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 602
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 7.35e-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: 46.55  E-value: 7.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354  106 REIVWLEREERARqhyeKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNR 181
Cdd:pfam05672   1 KPSAGTTDAEEAA----RILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKR 72
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
127-406 9.12e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  127 ERKKRLEEQRQKEERRRAAVEEK------RR--QRLEEDKERHEAVVRRTMERSQKPKQKHNRWSwgGSLHGSPSIHSAA 198
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmwLEdlDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKA--SKLRKPKLKKKEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  199 RRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAAScspiiMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTAS 278
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKS-----NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSS 1254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  279 YKKERERENVLFLTSGTRRAVSPSNPKARQPARsrlwlPSKSLPHLP-GTPRPTSSlppgSVKAAPAQVRPPSPGNIRPV 357
Cdd:PTZ00108 1255 EDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPP-----PSKRPDGESnGGSKPSSP----TKKKVKKRLEGSLAALKKKK 1325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 310750354  358 KREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPE 406
Cdd:PTZ00108 1326 KSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVD 1374
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
115-178 5.84e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 5.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354 115 ERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVR--RTMERSQKPKQK 178
Cdd:PRK00409 540 EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKelRQLQKGGYASVK 605
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
453-602 2.74e-20

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: 88.15  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  453 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 532
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQRK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750354  533 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 602
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 7.35e-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: 46.55  E-value: 7.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354  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 9.01e-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: 42.80  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354   87 DRQRLARERREEREKQLAAREIVWLErEERARQHYEKHLEERKKRLEEqrqkEERRRAAVEEKRRQR-LEEDKERHEAVV 165
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIYE----EERRREAEEERRKQQeMEERRRIQEQMR 559

                  ....*...
gi 310750354  166 RRTMERSQ 173
Cdd:pfam17380 560 KATEERSR 567
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
127-406 9.12e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  127 ERKKRLEEQRQKEERRRAAVEEK------RR--QRLEEDKERHEAVVRRTMERSQKPKQKHNRWSwgGSLHGSPSIHSAA 198
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEKLKNTtpkdmwLEdlDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKA--SKLRKPKLKKKEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  199 RRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAAScspiiMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTAS 278
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKS-----NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSS 1254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354  279 YKKERERENVLFLTSGTRRAVSPSNPKARQPARsrlwlPSKSLPHLP-GTPRPTSSlppgSVKAAPAQVRPPSPGNIRPV 357
Cdd:PTZ00108 1255 EDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPP-----PSKRPDGESnGGSKPSSP----TKKKVKKRLEGSLAALKKKK 1325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 310750354  358 KREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPE 406
Cdd:PTZ00108 1326 KSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVD 1374
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
115-178 5.84e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 5.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354 115 ERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVR--RTMERSQKPKQK 178
Cdd:PRK00409 540 EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKelRQLQKGGYASVK 605
PTZ00121 PTZ00121
MAEBL; Provisional
86-179 6.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750354   86 DDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVV 165
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
                          90
                  ....*....|....
gi 310750354  166 rrtmERSQKPKQKH 179
Cdd:PTZ00121 1752 ----DEEEKKKIAH 1761
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
112-174 8.73e-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: 8.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 310750354  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 9.21e-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: 38.10  E-value: 9.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 310750354  104 AAREIVWLEREERARQH--YEKHLEERKKRLEEQRQ-KEERRRAAVEEKRRQRLEE 156
Cdd:pfam09756  19 QQREAEEEEREEREKLEekREEEYKEREEREEEAEKeKEEEERKQEEEQERKEQEE 74
 
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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