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Conserved domains on  [gi|166197666|ref|NP_006599|]
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protein PHTF1 isoform a [Homo sapiens]

Protein Classification

PHTF domain-containing protein( domain architecture ID 10572778)

PHTF (putative homeodomain transcription factor) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHTF1-2_N pfam12129
Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of ...
 3-149 1.40e-83

Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of homeodomain containing proteins from animals, including PHTF1/2,eukaryotes, and is typically between 101 and 140 amino acids in length. PHTF proteins do not display any sequence similarity to known or predicted proteins, but their conservation among species suggests an essential function. The 84 kDa PHTF1 protein is an integral membrane protein, anchored to a cell membrane by six to eight trans-membrane domains, that is associated with a domain of the endoplasmic reticulum (ER) juxtaposed to the Golgi apparatus. It is present during meiosis and spermiogenesis, and, by the end of spermiogenesis, is released from the mature spermatozoon within the residual bodies. PHTF1 enhances the binding of FEM1B -feminization homolog 1B - to cell membranes. Fem-1 was initially identified in the signaling pathway for sex determination, as well as being implicated in apoptosis, but its biochemical role is still unclear, and neither FEM1B nor PHTF1 is directly implicated in apoptosis in spermatogenesis. It is the ANK domain of FEM1B that is necessary for the interaction with the N-terminal region of PHTF1.


:

Pssm-ID: 463466  Cd Length: 156  Bit Score: 262.27  E-value: 1.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197666    3 SNERDAISWYQKKIGAYDQQIWEKSIEQTQIKGLKNKPKKMGHIKPDLIDVDLIRGSTFAKAKPEIPWTSLTRKGLVRVV 82
Cdd:pfam12129   1 MKLDDAVAWYQKKIGTYDKQIWEKTVEQRILKGLTHVPKKTTKLKTELIDVDLVRGSSFPKAKPKQGWLTVTRLGIVRVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166197666   83 FFPLFSNWWIQVTSLRIFVWLLLLYFMQVIAIVLYLMM-------PIVNISEVLGPLCLMLLMGTVHCQIVSTQ 149
Cdd:pfam12129  81 FFPLYAQWWIQQTSFNIFLLLLLLYLLQLINVLLYQNTnfeedepHAIPLSEVLGPIALMLLLGTVHSQIVSTR 154
 
Name Accession Description Interval E-value
PHTF1-2_N pfam12129
Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of ...
 3-149 1.40e-83

Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of homeodomain containing proteins from animals, including PHTF1/2,eukaryotes, and is typically between 101 and 140 amino acids in length. PHTF proteins do not display any sequence similarity to known or predicted proteins, but their conservation among species suggests an essential function. The 84 kDa PHTF1 protein is an integral membrane protein, anchored to a cell membrane by six to eight trans-membrane domains, that is associated with a domain of the endoplasmic reticulum (ER) juxtaposed to the Golgi apparatus. It is present during meiosis and spermiogenesis, and, by the end of spermiogenesis, is released from the mature spermatozoon within the residual bodies. PHTF1 enhances the binding of FEM1B -feminization homolog 1B - to cell membranes. Fem-1 was initially identified in the signaling pathway for sex determination, as well as being implicated in apoptosis, but its biochemical role is still unclear, and neither FEM1B nor PHTF1 is directly implicated in apoptosis in spermatogenesis. It is the ANK domain of FEM1B that is necessary for the interaction with the N-terminal region of PHTF1.


Pssm-ID: 463466  Cd Length: 156  Bit Score: 262.27  E-value: 1.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197666    3 SNERDAISWYQKKIGAYDQQIWEKSIEQTQIKGLKNKPKKMGHIKPDLIDVDLIRGSTFAKAKPEIPWTSLTRKGLVRVV 82
Cdd:pfam12129   1 MKLDDAVAWYQKKIGTYDKQIWEKTVEQRILKGLTHVPKKTTKLKTELIDVDLVRGSSFPKAKPKQGWLTVTRLGIVRVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166197666   83 FFPLFSNWWIQVTSLRIFVWLLLLYFMQVIAIVLYLMM-------PIVNISEVLGPLCLMLLMGTVHCQIVSTQ 149
Cdd:pfam12129  81 FFPLYAQWWIQQTSFNIFLLLLLLYLLQLINVLLYQNTnfeedepHAIPLSEVLGPIALMLLLGTVHSQIVSTR 154
 
Name Accession Description Interval E-value
PHTF1-2_N pfam12129
Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of ...
 3-149 1.40e-83

Homeodomain containing protein PHTF1/2, N-terminal; This domain is found in a group of homeodomain containing proteins from animals, including PHTF1/2,eukaryotes, and is typically between 101 and 140 amino acids in length. PHTF proteins do not display any sequence similarity to known or predicted proteins, but their conservation among species suggests an essential function. The 84 kDa PHTF1 protein is an integral membrane protein, anchored to a cell membrane by six to eight trans-membrane domains, that is associated with a domain of the endoplasmic reticulum (ER) juxtaposed to the Golgi apparatus. It is present during meiosis and spermiogenesis, and, by the end of spermiogenesis, is released from the mature spermatozoon within the residual bodies. PHTF1 enhances the binding of FEM1B -feminization homolog 1B - to cell membranes. Fem-1 was initially identified in the signaling pathway for sex determination, as well as being implicated in apoptosis, but its biochemical role is still unclear, and neither FEM1B nor PHTF1 is directly implicated in apoptosis in spermatogenesis. It is the ANK domain of FEM1B that is necessary for the interaction with the N-terminal region of PHTF1.


Pssm-ID: 463466  Cd Length: 156  Bit Score: 262.27  E-value: 1.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166197666    3 SNERDAISWYQKKIGAYDQQIWEKSIEQTQIKGLKNKPKKMGHIKPDLIDVDLIRGSTFAKAKPEIPWTSLTRKGLVRVV 82
Cdd:pfam12129   1 MKLDDAVAWYQKKIGTYDKQIWEKTVEQRILKGLTHVPKKTTKLKTELIDVDLVRGSSFPKAKPKQGWLTVTRLGIVRVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166197666   83 FFPLFSNWWIQVTSLRIFVWLLLLYFMQVIAIVLYLMM-------PIVNISEVLGPLCLMLLMGTVHCQIVSTQ 149
Cdd:pfam12129  81 FFPLYAQWWIQQTSFNIFLLLLLLYLLQLINVLLYQNTnfeedepHAIPLSEVLGPIALMLLLGTVHSQIVSTR 154
 
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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