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Conserved domains on  [gi|530421030|ref|XP_005274536|]
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MAP7 domain-containing protein 2 isoform X8 [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 ...
 403-569 1.70e-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: 105.89  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  403 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 482
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  483 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 562
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 530421030  563 KRTRKSD 569
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 9.00e-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: 49.35  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530421030  112 VEEKRKQKLREEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 161-326 3.45e-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: 40.83  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 161 DGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSY--KSSPTRNI 238
Cdd:PTZ00449 512 EGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFpkDPKHPKDP 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 239 EKKKATSTSTSGAGDVGKEALSGGEASLVEKVKRGQRTATS--LPVvnfgSPLRRCEfsggiPKRPSSPVISKTatkayP 316
Cdd:PTZ00449 592 EEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSpkRPP----PPQRPSS-----PERPEGPKIIKS-----P 657

                        170
                 ....*....|
gi 530421030 317 QSPKTTKPPY 326
Cdd:PTZ00449 658 KPPKSPKPPF 667
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 403-569 1.70e-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: 105.89  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  403 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 482
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  483 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 562
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 530421030  563 KRTRKSD 569
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-146 9.00e-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: 49.35  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530421030  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 8.42e-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: 42.14  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   13 RPEGTARGTSLPGKIAEPGAVrTSQPNYRPQGMEGFLKSdERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQME 92
Cdd:TIGR02794  28 KPEPGGGAEIIQAVLVDPGAV-AQQANRIQQQKKPAAKK-EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530421030   93 ERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMMRRSLERTQ-QLELKKK 146
Cdd:TIGR02794 102 KAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkQAEEEAK 157
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 2.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 121
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          90       100
                  ....*....|....*....|....*
gi 530421030  122 EEEERLEAMMRRSLERTQQLELKKK 146
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 161-326 3.45e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 161 DGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSY--KSSPTRNI 238
Cdd:PTZ00449 512 EGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFpkDPKHPKDP 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 239 EKKKATSTSTSGAGDVGKEALSGGEASLVEKVKRGQRTATS--LPVvnfgSPLRRCEfsggiPKRPSSPVISKTatkayP 316
Cdd:PTZ00449 592 EEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSpkRPP----PPQRPSS-----PERPEGPKIIKS-----P 657

                        170
                 ....*....|
gi 530421030 317 QSPKTTKPPY 326
Cdd:PTZ00449 658 KPPKSPKPPF 667
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 53-119 4.65e-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: 4.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530421030  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 119
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 ...
 403-569 1.70e-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: 105.89  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  403 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 482
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030  483 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 562
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143


                  ....*..
gi 530421030  563 KRTRKSD 569
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-146 9.00e-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: 49.35  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   33 VRTSQPNYRPQGMEGFLKSDERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraA 111
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----A 538

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530421030  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 8.42e-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: 42.14  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   13 RPEGTARGTSLPGKIAEPGAVrTSQPNYRPQGMEGFLKSdERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQME 92
Cdd:TIGR02794  28 KPEPGGGAEIIQAVLVDPGAV-AQQANRIQQQKKPAAKK-EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530421030   93 ERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMMRRSLERTQ-QLELKKK 146
Cdd:TIGR02794 102 KAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkQAEEEAK 157
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 2.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 121
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          90       100
                  ....*....|....*....|....*
gi 530421030  122 EEEERLEAMMRRSLERTQQLELKKK 146
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 53-148 2.31e-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: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   53 ERQRLAKERRE--EREKCLAAREQQILEKQKRA-RLQYEKQMEERWRKLEE-QRQREDQKRAAVEEKRKQKlrEEEERLE 128
Cdd:pfam15346  46 ARKIMEKQVLEelEREREAELEEERRKEEEERKkREELERILEENNRKIEEaQRKEAEERLAMLEEQRRMK--EERQRRE 123

                          90       100
                  ....*....|....*....|
gi 530421030  129 AMMRRSLERTQQLELKKKYS 148
Cdd:pfam15346 124 KEEEEREKREQQKILNKKNS 143
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 161-326 3.45e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 161 DGLAASTLPPDAGTTAAAAESTNACDKLSTSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSY--KSSPTRNI 238
Cdd:PTZ00449 512 EGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFpkDPKHPKDP 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 239 EKKKATSTSTSGAGDVGKEALSGGEASLVEKVKRGQRTATS--LPVvnfgSPLRRCEfsggiPKRPSSPVISKTatkayP 316
Cdd:PTZ00449 592 EEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSpkRPP----PPQRPSS-----PERPEGPKIIKS-----P 657

                        170
                 ....*....|
gi 530421030 317 QSPKTTKPPY 326
Cdd:PTZ00449 658 KPPKSPKPPF 667
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 19-119 3.46e-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: 40.88  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   19 RGTSLPGKIAEPGAVRTSQPNYRPQGMEGFLKSDERQ--RLAKERREEREKCLAAREQQilEKQKRARLQYEKQMEERWR 96
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmeRVRLEEQERQQQVERLRQQE--EERKRKKLELEKEKRDRKR 488

                          90       100
                  ....*....|....*....|....*...
gi 530421030   97 KLEEQR-----QREDQKRAAVEEKRKQK 119
Cdd:pfam17380 489 AEEQRRkilekELEERKQAMIEEERKRK 516
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 53-119 4.65e-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: 4.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530421030  53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 119
Cdd:cd16269  197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 190-321 4.69e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030 190 TSTMSLPKPTEPPMNKRLSSSTVAISYSPDRAPLGPLNPSYKSSPTRNIEKKKATSTSTSGAGDVGKEALSGGEASLVEK 269
Cdd:PTZ00449 631 KSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPET 710

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530421030 270 VKRGQRTATSLPVVNFGSPlrrcEFSGGIPKRPSSPVISKTATKAYPQSPKT 321
Cdd:PTZ00449 711 PGTPFTTPRPLPPKLPRDE----EFPFEPIGDPDAEQPDDIEFFTPPEEERT 758
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 53-146 6.18e-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: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   53 ERQRLAKERREEREkclAAREQQILEKQK------------RARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKL 120
Cdd:pfam17380 386 ERQQKNERVRQELE---AARKVKILEEERqrkiqqqkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462

                          90       100
                  ....*....|....*....|....*.
gi 530421030  121 REEEERLEAMMRRSLERTQQLELKKK 146
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKR 488
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 52-119 6.71e-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: 39.52  E-value: 6.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530421030   52 DERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 119
Cdd:pfam13868  58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 50-119 7.08e-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: 38.48  E-value: 7.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKERREEREKclaarEQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 119
Cdd:pfam09756   6 KKRAKLELKEAKRQQREA-----EEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERK 70
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 54-107 8.29e-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: 8.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530421030   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 ...
 53-145 8.39e-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: 39.25  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   53 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQM---EERWRKL----EEQRQREDQKRAAVEEKRKQKLREEEE 125
Cdd:pfam15558  51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQViekESRWREQaedqENQRQEKLERARQEAEQRKQCQEQRLK 130

                          90       100
                  ....*....|....*....|
gi 530421030  126 RLEAMMRRSLERTQQLELKK 145
Cdd:pfam15558 131 EKEEELQALREQNSLQLQER 150
PTZ00121 PTZ00121
MAEBL; Provisional
 50-118 8.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 118
Cdd:PTZ00121 1669 KAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 8.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEA 129
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530

                          90
                  ....*....|....*..
gi 530421030  130 MMRRSLERTQQLELKKK 146
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKK 1547
PTZ00121 PTZ00121
MAEBL; Provisional
 50-146 9.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530421030   50 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLE 128
Cdd:PTZ00121 1641 KEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720

                          90
                  ....*....|....*...
gi 530421030  129 AMMRRSLERTQQLELKKK 146
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKE 1738
 
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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