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Conserved domains on  [gi|568906675|ref|XP_006496197|]
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RUN and FYVE domain-containing protein 4 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 371-413 1.50e-10

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


:

Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 56.36  E-value: 1.50e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSVDYK--------KRERCCPTC 413
Cdd:cd15745    1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLvlsvpdtcIYLRVCKTC 51
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 275-354 8.32e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


:

Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.18  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  275 QLAKEQAQCQEQLRAQEAELQALQEQLsrcQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:pfam03938  23 QLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQDK 99
CCDC22 super family cl25503
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 63-364 4.92e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   63 SRGEQLQEPdTGGTSCLQDATREDRTPDLCKPLQPSHLPTflEEKREDSRSLsCPQSTWETEREGFQLDQKDGGPKPRKF 142
Cdd:pfam05667 111 ESSEAADQP-VGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRAL-RPFHTQTLVLPGRKGKTLKNSKELKEF 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  143 LENSTASIQQQRSRAKDVKMQLTGRKVEGKGSLSGTEDQRTTEGIQKRAADWDLGQGLMAPGLQGREDA--ELGYRCEWN 220
Cdd:pfam05667 187 YSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQlrSAALAGTEA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  221 QPDVLRQSWVLGTKKSSPTEKPQEWTGVTSGTMQEDGSEVPLQQEvikDPGYGLQLAKEQAQCQEQLRAQEAELQALQEQ 300
Cdd:pfam05667 267 TSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNE---APAATSSPPTKVETEEELQQQREEELEELQEQ 343

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906675  301 LSRCQ-------KERALLQVKLEQKQQEAERRDAMyQTELEGQRDLvqamKRRVLELIHEKDLQWQRLQQL 364
Cdd:pfam05667 344 LEDLEssiqeleKEIKKLESSIKQVEEELEELKEQ-NEELEKQYKV----KKKTLDLLPDAEENIAKLQAL 409
 
Name Accession Description Interval E-value
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 371-413 1.50e-10

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 56.36  E-value: 1.50e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSVDYK--------KRERCCPTC 413
Cdd:cd15745    1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLvlsvpdtcIYLRVCKTC 51
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 371-416 1.59e-07

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 48.15  E-value: 1.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568906675  371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS---------VDYKKRERCCPTCAQQ 416
Cdd:pfam01363  11 VCMICSKPFTFFRRRHHCRNCGRVFCSACSskkisllpeLGSNKPVRVCDACYDT 65
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 371-415 1.17e-06

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 45.89  E-value: 1.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568906675   371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS--------VDYKKRERCCPTCAQ 415
Cdd:smart00064  12 NCMGCGKEFNLTKRRHHCRNCGRIFCSKCSskkaplpkLGIERPVRVCDDCYE 64
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 275-354 8.32e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.18  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  275 QLAKEQAQCQEQLRAQEAELQALQEQLsrcQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:pfam03938  23 QLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQDK 99
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 275-353 9.38e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 9.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   275 QLAKEQAQCQEQLRAQEAELQALQEQLSR-----CQKERALLQVKLEQKQQEAERRDAMYQTELEG-QRDLVQAMKRRVL 348
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKrQQEELQKILDKIN 101


                   ....*
gi 568906675   349 ELIHE 353
Cdd:smart00935 102 KAIKE 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-363 1.00e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQ------TELEGQRDLVQAMKRRVL 348
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelARLEQDIARLEERRRELE 315

                         90
                 ....*....|....*
gi 568906675 349 ELIHEKDLQWQRLQQ 363
Cdd:COG1196  316 ERLEELEEELAELEE 330
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 282-365 1.17e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.94  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 282 QCQEQLRAQeAELQALQEQ-LSRCQKERALLQVKLEQKQQEAerrDAMYQTELEGQRDLVQAMK------RRVLELIHEK 354
Cdd:cd16855   37 QYQESQKIQ-AQLQQLQQQpQNERIELEQQLQQQKEQLEQLL---NAKAQELLQLRMELADKFKktiqllSKLQSRVLDE 112

                         90
                 ....*....|..
gi 568906675 355 DL-QWQRLQQLS 365
Cdd:cd16855  113 ELiQWKRQQQLA 124
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 275-366 2.56e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQ---TELEGQRDLVQAMKRRVLELI 351
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLE 392

                           90
                   ....*....|....*
gi 568906675   352 HEKDLQWQRLQQLST 366
Cdd:TIGR02168  393 LQIASLNNEIERLEA 407
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 63-364 4.92e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   63 SRGEQLQEPdTGGTSCLQDATREDRTPDLCKPLQPSHLPTflEEKREDSRSLsCPQSTWETEREGFQLDQKDGGPKPRKF 142
Cdd:pfam05667 111 ESSEAADQP-VGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRAL-RPFHTQTLVLPGRKGKTLKNSKELKEF 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  143 LENSTASIQQQRSRAKDVKMQLTGRKVEGKGSLSGTEDQRTTEGIQKRAADWDLGQGLMAPGLQGREDA--ELGYRCEWN 220
Cdd:pfam05667 187 YSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQlrSAALAGTEA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  221 QPDVLRQSWVLGTKKSSPTEKPQEWTGVTSGTMQEDGSEVPLQQEvikDPGYGLQLAKEQAQCQEQLRAQEAELQALQEQ 300
Cdd:pfam05667 267 TSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNE---APAATSSPPTKVETEEELQQQREEELEELQEQ 343

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906675  301 LSRCQ-------KERALLQVKLEQKQQEAERRDAMyQTELEGQRDLvqamKRRVLELIHEKDLQWQRLQQL 364
Cdd:pfam05667 344 LEDLEssiqeleKEIKKLESSIKQVEEELEELKEQ-NEELEKQYKV----KKKTLDLLPDAEENIAKLQAL 409
 
Name Accession Description Interval E-value
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 371-413 1.50e-10

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 56.36  E-value: 1.50e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSVDYK--------KRERCCPTC 413
Cdd:cd15745    1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLvlsvpdtcIYLRVCKTC 51
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 371-414 4.83e-09

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: 52.15  E-value: 4.83e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSV--------DYKKRERCCPTCA 414
Cdd:cd00065    1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSkklplpsfGSGKPVRVCDSCY 52
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 371-416 1.59e-07

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 48.15  E-value: 1.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568906675  371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS---------VDYKKRERCCPTCAQQ 416
Cdd:pfam01363  11 VCMICSKPFTFFRRRHHCRNCGRVFCSACSskkisllpeLGSNKPVRVCDACYDT 65
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
 371-414 2.14e-07

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 47.55  E-value: 2.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSVDY------KKRERCCPTCA 414
Cdd:cd15726    9 HCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYvltahgGKKERCCKACF 58
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
 372-413 6.66e-07

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 46.18  E-value: 6.66e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568906675 372 CIGCNKVFRRLSRRYPCRLCGGLVCHACSVDYKKRERCCPTC 413
Cdd:cd15716   13 CPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPLHIRCCHHC 54
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 371-415 1.17e-06

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 45.89  E-value: 1.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568906675   371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS--------VDYKKRERCCPTCAQ 415
Cdd:smart00064  12 NCMGCGKEFNLTKRRHHCRNCGRIFCSKCSskkaplpkLGIERPVRVCDDCYE 64
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 275-354 8.32e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.18  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  275 QLAKEQAQCQEQLRAQEAELQALQEQLsrcQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:pfam03938  23 QLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQDK 99
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 275-353 9.38e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 9.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   275 QLAKEQAQCQEQLRAQEAELQALQEQLSR-----CQKERALLQVKLEQKQQEAERRDAMYQTELEG-QRDLVQAMKRRVL 348
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKrQQEELQKILDKIN 101


                   ....*
gi 568906675   349 ELIHE 353
Cdd:smart00935 102 KAIKE 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-363 1.00e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQ------TELEGQRDLVQAMKRRVL 348
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelARLEQDIARLEERRRELE 315

                         90
                 ....*....|....*
gi 568906675 349 ELIHEKDLQWQRLQQ 363
Cdd:COG1196  316 ERLEELEEELAELEE 330
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
 371-413 1.30e-04

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 39.67  E-value: 1.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS------VDYKKRERCCPTC 413
Cdd:cd15721    9 HCQQCEKEFSLSRRKHHCRNCGGIFCNSCSdntmplPSSAKPVRVCDTC 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-365 1.38e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 284 QEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAmyqtELEGQRDLVQAMKRRVLELIHEKDLQWQRLQQ 363
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEERRRE 313


                 ..
gi 568906675 364 LS 365
Cdd:COG1196  314 LE 315
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-364 1.67e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         90
                 ....*....|
gi 568906675 355 DLQWQRLQQL 364
Cdd:COG1196  393 RAAAELAAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-363 3.33e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQT------ELEGQRDLVQAMKRRVL 348
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeeleEAEAELAEAEEALLEAE 371

                         90
                 ....*....|....*
gi 568906675 349 ELIHEKDLQWQRLQQ 363
Cdd:COG1196  372 AELAEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-365 3.79e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                         90
                 ....*....|.
gi 568906675 355 DLQWQRLQQLS 365
Cdd:COG1196  400 AQLEELEEAEE 410
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
 368-400 4.28e-04

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 38.18  E-value: 4.28e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568906675 368 APGHCIGCNKVFRRLSRRYPCRLCGGLVCHACS 400
Cdd:cd15733    6 AASHCFGCDCEFWLAKRKHHCRNCGNVFCADCS 38
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 371-413 6.93e-04

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 38.12  E-value: 6.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACSVD------YKKRERCCPTC 413
Cdd:cd15758   14 HCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNelalpsYPKPVRVCDSC 62
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
284-369 1.01e-03

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 39.95  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 284 QEQLRAQEAELQALQEQLSrcqkerallqvKLEQKQQEAErrdamyqtELEGQRDLVQAmKRRVLELIHEKDLQWQR-LQ 362
Cdd:COG3166   44 QGQIAQQQARNAALQQEIA-----------KLDKQIAEIK--------ELKKQKAELLA-RLQVIEQLQQSRPPWVHlLD 103


                 ....*..
gi 568906675 363 QLSTVAP 369
Cdd:COG3166  104 ELARLLP 110
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 282-365 1.17e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.94  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 282 QCQEQLRAQeAELQALQEQ-LSRCQKERALLQVKLEQKQQEAerrDAMYQTELEGQRDLVQAMK------RRVLELIHEK 354
Cdd:cd16855   37 QYQESQKIQ-AQLQQLQQQpQNERIELEQQLQQQKEQLEQLL---NAKAQELLQLRMELADKFKktiqllSKLQSRVLDE 112

                         90
                 ....*....|..
gi 568906675 355 DL-QWQRLQQLS 365
Cdd:cd16855  113 ELiQWKRQQQLA 124
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
 372-413 1.34e-03

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 36.96  E-value: 1.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568906675 372 CIGCNKV-FRRLSRRYPCRLCGGLVCHACS-------VDYKKRERCCPTC 413
Cdd:cd15717   11 CMHCKKTkFTAINRRHHCRKCGAVVCGACSskkfllpHQSSKPLRVCDTC 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-368 1.52e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413

                         90
                 ....*....|....
gi 568906675 355 DLQWQRLQQLSTVA 368
Cdd:COG1196  414 ERLERLEEELEELE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 275-366 2.56e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQ---TELEGQRDLVQAMKRRVLELI 351
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLE 392

                           90
                   ....*....|....*
gi 568906675   352 HEKDLQWQRLQQLST 366
Cdd:TIGR02168  393 LQIASLNNEIERLEA 407
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-364 2.57e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQvKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                         90
                 ....*....|
gi 568906675 355 DLQWQRLQQL 364
Cdd:COG1196  445 EEAAEEEAEL 454
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
268-363 2.88e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 268 KDPGYGLQLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAM------YQTELEGQRDLVQ 341
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqllplYQELEALEAELAE 143

                         90       100
                 ....*....|....*....|..
gi 568906675 342 AMKRrvLELIHEKDLQWQRLQQ 363
Cdd:COG4717  144 LPER--LEELEERLEELRELEE 163
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 275-346 3.57e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 3.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRR 346
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 275-363 3.66e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKE--RALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKrRVLELIH 352
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQK-RLMEMAE 473

                          90
                  ....*....|.
gi 568906675  353 EKDLQWQRLQQ 363
Cdd:pfam15709 474 EERLEYQRQKQ 484
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 63-364 4.92e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675   63 SRGEQLQEPdTGGTSCLQDATREDRTPDLCKPLQPSHLPTflEEKREDSRSLsCPQSTWETEREGFQLDQKDGGPKPRKF 142
Cdd:pfam05667 111 ESSEAADQP-VGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRAL-RPFHTQTLVLPGRKGKTLKNSKELKEF 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  143 LENSTASIQQQRSRAKDVKMQLTGRKVEGKGSLSGTEDQRTTEGIQKRAADWDLGQGLMAPGLQGREDA--ELGYRCEWN 220
Cdd:pfam05667 187 YSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQlrSAALAGTEA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  221 QPDVLRQSWVLGTKKSSPTEKPQEWTGVTSGTMQEDGSEVPLQQEvikDPGYGLQLAKEQAQCQEQLRAQEAELQALQEQ 300
Cdd:pfam05667 267 TSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNE---APAATSSPPTKVETEEELQQQREEELEELQEQ 343

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906675  301 LSRCQ-------KERALLQVKLEQKQQEAERRDAMyQTELEGQRDLvqamKRRVLELIHEKDLQWQRLQQL 364
Cdd:pfam05667 344 LEDLEssiqeleKEIKKLESSIKQVEEELEELKEQ-NEELEKQYKV----KKKTLDLLPDAEENIAKLQAL 409
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-363 5.20e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  284 QEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQE----AERRDAMYQTELEGQRDLVQAMKRRVLELIHEKDLQwQ 359
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-E 769


                  ....
gi 568906675  360 RLQQ 363
Cdd:COG4913   770 NLEE 773
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
 371-414 5.54e-03

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 34.97  E-value: 5.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS---------VDYKKRERCCPTCA 414
Cdd:cd15760    7 RCDVCRKKFGLFKRRHHCRNCGDSFCSEHSsrriplphlGPLGVPQRVCDRCF 59
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
 371-400 6.57e-03

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 35.01  E-value: 6.57e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 568906675 371 HCIGCNKVFRRLSRRYPCRLCGGLVCHACS 400
Cdd:cd15731   13 QCMACSAPFTVLRRRHHCRNCGKIFCSRCS 42
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-364 6.76e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQ----------KQQEAERRDAMYQTELEGQRDLVQAMK 344
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarleeRRRELEERLEELEEELAELEEELEELE 336

                         90       100
                 ....*....|....*....|
gi 568906675 345 RRVLELIHEKDLQWQRLQQL 364
Cdd:COG1196  337 EELEELEEELEEAEEELEEA 356
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
 372-415 6.84e-03

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 34.99  E-value: 6.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568906675 372 CIGCNKVFRRLSRRYPCRLCGGLVCHACS--------VDYKKRERCCPTCAQ 415
Cdd:cd15725   11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCnqeipgkfIGYPGDLRVCTYCCK 62
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 275-350 7.08e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 7.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLEL 350
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
275-364 7.43e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 7.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQ---QEAERRDAMYQTELEGQRDLVQAMKRRVLELI 351
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90
                 ....*....|...
gi 568906675 352 HEKDLQWQRLQQL 364
Cdd:COG4372  122 KERQDLEQQRKQL 134
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 275-343 7.44e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 7.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRdamyQTELEGQRDLVQAM 343
Cdd:COG3883   27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGER 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
277-364 7.66e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675  277 AKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVkleqkqQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEKDL 356
Cdd:COG4913   247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRL------WFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320


                  ....*...
gi 568906675  357 QWQRLQQL 364
Cdd:COG4913   321 LREELDEL 328
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
 372-415 8.97e-03

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 34.64  E-value: 8.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568906675 372 CIGCNKVFRRLSRRYPCRLCGGLVCHAC-----SVDY--KKRERCCPTCAQ 415
Cdd:cd15729   16 CMQCEVKFTFTKRRHHCRACGKVLCSACcslkaRLEYldNKEARVCVPCYQ 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 275-363 9.68e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906675 275 QLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEK 354
Cdd:COG3883  126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205


                 ....*....
gi 568906675 355 DLQWQRLQQ 363
Cdd:COG3883  206 AAAEAAAAA 214
 
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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