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Conserved domains on  [gi|1729094467|ref|XP_030436499|]
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melanophilin isoform X6 [Gopherus evgoodei]

Protein Classification

melanophilin( domain architecture ID 10491883)

melanophilin acts as a Rab effector protein that is involved in melanosome transport and serves as link between melanosome-bound RAB27A and the motor protein MYO5A

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
8-125 2.35e-73

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


:

Pssm-ID: 426716  Cd Length: 118  Bit Score: 230.34  E-value: 2.35e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467   8 SKLTDEEAKHVWEVVQRDFDLRKKEEDRLEELKCKLEKEGTKRELLSNQSHLNETHCVHCLQPFKFLVNSKRQCLDCHFY 87
Cdd:pfam02318   1 SKLTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLDKESSKRELLGNQAHLGETHCIRCLQPFGFLVNSKRQCLDCRKN 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1729094467  88 TCKNCSRYNKKEQGWICDPCRLSRIVKIGSLEWYYEHV 125
Cdd:pfam02318  81 VCKKCGVYNKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
Rab_eff_C super family cl12299
Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab ...
428-591 3.61e-16

Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab effector proteins MyRIP and melanophilin.


The actual alignment was detected with superfamily member pfam04698:

Pssm-ID: 461398 [Multi-domain]  Cd Length: 717  Bit Score: 82.23  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 428 QKVCTTAGKTSGLDQTPRDLEECAR--HSGTTDSELSELEDKVASAAMQLQRAESEVSDIESRIAALSAAGLTVKPVEKp 505
Cdd:pfam04698 557 ENVYLTAGTVYGLEGQLTELEDAARciSSVTAETELADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNVAPCVR- 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 506 kkkystqlfmLQPPRNVGSGQGDQSTDSSEMASpndfKVMSMPQVLRRKFNSSLEIAdgDESFDRNSIYRGSLTQRNPNG 585
Cdd:pfam04698 636 ----------LTRKREQKQRSQVQTIDTSRQQR----RKLPAPPVKAEKIEASSVTT--VKTFNRNFILQGSLTQRTKER 699

                  ....*.
gi 1729094467 586 KNRKAD 591
Cdd:pfam04698 700 KSTAKD 705
 
Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
8-125 2.35e-73

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


Pssm-ID: 426716  Cd Length: 118  Bit Score: 230.34  E-value: 2.35e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467   8 SKLTDEEAKHVWEVVQRDFDLRKKEEDRLEELKCKLEKEGTKRELLSNQSHLNETHCVHCLQPFKFLVNSKRQCLDCHFY 87
Cdd:pfam02318   1 SKLTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLDKESSKRELLGNQAHLGETHCIRCLQPFGFLVNSKRQCLDCRKN 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1729094467  88 TCKNCSRYNKKEQGWICDPCRLSRIVKIGSLEWYYEHV 125
Cdd:pfam02318  81 VCKKCGVYNKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
FYVE_SlaC2-a cd15752
FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; ...
62-137 1.54e-45

FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; SlaC2-a, also termed melanophilin, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va. SlaC2-a belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain.


Pssm-ID: 277291  Cd Length: 76  Bit Score: 155.34  E-value: 1.54e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729094467  62 THCVHCLQPFKFLVNSKRQCLDCHFYTCKNCSRYNKKEQGWICDPCRLSRIVKIGSLEWYYEHVRSRFRRFGSAKV 137
Cdd:cd15752     1 THCARCLQPFQFLLNSGRQCLDCGLRTCKSCSRYHPEEQGWVCDPCHLARVVKIGSLEWYYNHVRARFKRFGSAKV 76
Rab_eff_C pfam04698
Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab ...
428-591 3.61e-16

Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab effector proteins MyRIP and melanophilin.


Pssm-ID: 461398 [Multi-domain]  Cd Length: 717  Bit Score: 82.23  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 428 QKVCTTAGKTSGLDQTPRDLEECAR--HSGTTDSELSELEDKVASAAMQLQRAESEVSDIESRIAALSAAGLTVKPVEKp 505
Cdd:pfam04698 557 ENVYLTAGTVYGLEGQLTELEDAARciSSVTAETELADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNVAPCVR- 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 506 kkkystqlfmLQPPRNVGSGQGDQSTDSSEMASpndfKVMSMPQVLRRKFNSSLEIAdgDESFDRNSIYRGSLTQRNPNG 585
Cdd:pfam04698 636 ----------LTRKREQKQRSQVQTIDTSRQQR----RKLPAPPVKAEKIEASSVTT--VKTFNRNFILQGSLTQRTKER 699

                  ....*.
gi 1729094467 586 KNRKAD 591
Cdd:pfam04698 700 KSTAKD 705
 
Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
8-125 2.35e-73

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


Pssm-ID: 426716  Cd Length: 118  Bit Score: 230.34  E-value: 2.35e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467   8 SKLTDEEAKHVWEVVQRDFDLRKKEEDRLEELKCKLEKEGTKRELLSNQSHLNETHCVHCLQPFKFLVNSKRQCLDCHFY 87
Cdd:pfam02318   1 SKLTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLDKESSKRELLGNQAHLGETHCIRCLQPFGFLVNSKRQCLDCRKN 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1729094467  88 TCKNCSRYNKKEQGWICDPCRLSRIVKIGSLEWYYEHV 125
Cdd:pfam02318  81 VCKKCGVYNKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
FYVE_SlaC2-a cd15752
FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; ...
62-137 1.54e-45

FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; SlaC2-a, also termed melanophilin, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va. SlaC2-a belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain.


Pssm-ID: 277291  Cd Length: 76  Bit Score: 155.34  E-value: 1.54e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729094467  62 THCVHCLQPFKFLVNSKRQCLDCHFYTCKNCSRYNKKEQGWICDPCRLSRIVKIGSLEWYYEHVRSRFRRFGSAKV 137
Cdd:cd15752     1 THCARCLQPFQFLLNSGRQCLDCGLRTCKSCSRYHPEEQGWVCDPCHLARVVKIGSLEWYYNHVRARFKRFGSAKV 76
FYVE_SlaC2-c cd15753
FYVE-related domain found in Slp homolog lacking C2 domains c (SlaC2-c) and similar proteins; ...
64-111 3.02e-18

FYVE-related domain found in Slp homolog lacking C2 domains c (SlaC2-c) and similar proteins; SlaC2-c, also termed Rab effector MyRIP, or exophilin-8, or myosin-VIIa- and Rab-interacting protein, or synaptotagmin-like protein lacking C2 domains c, is a GTP-bound form of Rab27A-, myosin Va/VIIa-, and actin-binding protein mainly present on retinal melanosomes and secretory granules. It may play a role in insulin granule exocytosis. It is also involved in the control of isoproterenol (IPR)-induced amylase release from parotid acinar cells. SlaC2-c belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-c are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-c has a middle myosin-binding domain and a C-terminal actin-binding domain.


Pssm-ID: 277292  Cd Length: 49  Bit Score: 78.60  E-value: 3.02e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1729094467  64 CVHCLQPFKFLVNSKRQCLDCHFYTCKNCSRYNKKEQGWICDPCRLSR 111
Cdd:cd15753     2 CMRCCSPFTFLFNRKRQCRDCKFNVCKSCASYDKKEKGWTCNVCQKQR 49
Rab_eff_C pfam04698
Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab ...
428-591 3.61e-16

Rab effector MyRIP/melanophilin C-terminus; This domain is found at the C-terminus of the Rab effector proteins MyRIP and melanophilin.


Pssm-ID: 461398 [Multi-domain]  Cd Length: 717  Bit Score: 82.23  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 428 QKVCTTAGKTSGLDQTPRDLEECAR--HSGTTDSELSELEDKVASAAMQLQRAESEVSDIESRIAALSAAGLTVKPVEKp 505
Cdd:pfam04698 557 ENVYLTAGTVYGLEGQLTELEDAARciSSVTAETELADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNVAPCVR- 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729094467 506 kkkystqlfmLQPPRNVGSGQGDQSTDSSEMASpndfKVMSMPQVLRRKFNSSLEIAdgDESFDRNSIYRGSLTQRNPNG 585
Cdd:pfam04698 636 ----------LTRKREQKQRSQVQTIDTSRQQR----RKLPAPPVKAEKIEASSVTT--VKTFNRNFILQGSLTQRTKER 699

                  ....*.
gi 1729094467 586 KNRKAD 591
Cdd:pfam04698 700 KSTAKD 705
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
63-107 2.79e-05

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 41.75  E-value: 2.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1729094467  63 HCVHCLQPFKFLvNSKRQCLDCHFYTCKNCS-------RYNKKEQGWICDPC 107
Cdd:cd00065     1 RCMLCGKKFSLF-RRRHHCRRCGRVFCSKCSskklplpSFGSGKPVRVCDSC 51
FYVE_Slp3_4_5 cd15747
FYVE-related domain found in the synaptotagmin-like proteins 3, 4, 5; The synaptotagmin-like ...
63-107 1.02e-03

FYVE-related domain found in the synaptotagmin-like proteins 3, 4, 5; The synaptotagmin-like proteins 1-5 (Slp1-5) family belongs to the carboxyl-terminal-type (C-type) tandem C2 proteins superfamily, which also contains the synaptotagmin and the Doc2 families. Slp proteins are putative membrane trafficking proteins that are characterized by the presence of a unique N-terminal Slp homology domain (SHD), and C-terminal tandem C2 domains (known as the C2A domain and C2B domain). The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2. The SHD1 and SHD2 of Slp3, Slp4 and Slp5 are separated by a putative FYVE zinc finger. By contrast, Slp1 and Slp2 lack such zinc finger and their SHD1 and SHD2 are linked together. This model corresponds to the FYVE zinc finger. At this point, Slp1 and Slp2 are not included in this model. Moreover, the FYVE domains of Slp3, Slp4 and Slp5 resemble a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277286  Cd Length: 48  Bit Score: 37.28  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1729094467  63 HCVHCLQPFKFLVNSKRQCLDCHFYTCKNCSRYNKKEQGWICDPC 107
Cdd:cd15747     2 ICARCREKLGFIFNRGARCPKCSHKVCKKCRVLTSNTGKWLCTVC 46
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
63-109 2.38e-03

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 36.18  E-value: 2.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1729094467  63 HCVHCLQPFKFLvNSKRQCLDCHFYTCKNCSRyNKKEQGWICDPCRL 109
Cdd:cd15750     2 PCESCGAKFSVF-KRKRTCADCKRYFCSNCLS-KEERGRRRCRRCRA 46
PHD2_Snt2p_like cd15498
PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
64-107 6.95e-03

PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; This group corresponds to Snt2p and similar proteins. Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the second canonical Cys4HisCys3 PHD finger.


Pssm-ID: 276973  Cd Length: 55  Bit Score: 35.14  E-value: 6.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1729094467  64 CVHCLQPFKFLVNSKRQCLDC----HF--Y----TCKNCSRYNKKEQGWICDPC 107
Cdd:cd15498     2 CSVCSEQFASNFNTSLSCYNCglnvHAscYgitvPGKMNKVKNLKSYKWLCDPC 55
 
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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