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Conserved domains on  [gi|2024499903|ref|XP_040526816|]
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protein RUFY3 isoform X5 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 4.88e-101

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


:

Pssm-ID: 439058  Cd Length: 156  Bit Score: 304.23  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
570-619 7.93e-22

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


:

Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 88.63  E-value: 7.93e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499903 570 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 619
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-500 7.27e-10

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 7.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903  440 LRALKHELSFKLQSS--DMGVKQKS--ELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWS 500
Cdd:TIGR02168  815 LNEEAANLRERLESLerRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
flhF super family cl35529
flagellar biosynthesis protein FlhF;
4-128 6.40e-05

flagellar biosynthesis protein FlhF;


The actual alignment was detected with superfamily member PRK06995:

Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499903  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 4.88e-101

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 304.23  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
143-266 2.56e-46

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 426965  Cd Length: 136  Bit Score: 159.78  E-value: 2.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 143 QFFVVMEHCLKHGLKAKKT-----------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLAL 211
Cdd:pfam02759   1 SLCAALEALLSHGLKRKALsaslsliegyyGLLPERSFWDLLERVGKLVPPAEELLSSVQALEQIHTSDGRGRAWIRLAL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 212 MQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 266
Cdd:pfam02759  81 NEKLLEQWLNLLLSNKELLSKYYEPWALLRDPEFVeILLGLLVGLSALDFNLCLDL 136
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
570-619 7.93e-22

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 88.63  E-value: 7.93e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499903 570 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 619
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
203-265 2.04e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.19  E-value: 2.04e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499903  203 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 265
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
568-622 1.41e-11

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: 60.14  E-value: 1.41e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903  568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCHKQL 622
Cdd:smart00064  10 VSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
568-622 1.38e-10

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: 57.39  E-value: 1.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCHKQL 622
Cdd:pfam01363   9 ATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-500 7.27e-10

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: 62.38  E-value: 7.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903  440 LRALKHELSFKLQSS--DMGVKQKS--ELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWS 500
Cdd:TIGR02168  815 LNEEAANLRERLESLerRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
291-497 7.53e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.96  E-value: 7.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKV 370
Cdd:COG1196    719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  371 TKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFK 450
Cdd:COG1196    799 EEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDE 878
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024499903  451 LQSSdmgVKQKSELNSRLEEKTNQMAATIKQLE-QRSHLELELKRERE 497
Cdd:COG1196    879 LKEL---EEEKEELEEELRELESELAELKEEIEkLRERLEELEAKLER 923
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
317-509 1.49e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 430825 [Multi-domain]  Cd Length: 305  Bit Score: 53.59  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkvtkdrtadgQALTEARKQLKEETQLRL 396
Cdd:pfam09787  41 GSTALSLELDELRQERDLLREELQQLNQQIEQLRTELQELEAQQQEEAESSR----------EQLQDLEEQLATERQARR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 397 DVEKELEaqigmRQEMELamKMLEKDVCEKQDALVA-LRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLEEKTNQM 475
Cdd:pfam09787 111 EAEAELE-----RLQEEL--RYLEEELRRTKATLQSrIKDREAEIEKLRNQLTNKSQSS----SSQSELENRLHQLTESL 179
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024499903 476 AATIKQLE----QRSHLELELKReRERWSHSHQSSQGN 509
Cdd:pfam09787 180 IQKQTMLEalstEKNSLVLQLER-LEQQIKELQGEASN 216
flhF PRK06995
flagellar biosynthesis protein FlhF;
4-128 6.40e-05

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499903  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-497 9.65e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTKDRTADGQALTEA-RKQLKEETQLR 395
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA----IEELKKAKGKCPVCGRELTEEhRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 396 L-DVEKELEAQIGMRQEMELAMKMLEKdVCEKQDALVALRQQLDDLRALKHELS-FKLQSsdmgVKQKSELNSRLEEKTN 473
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKkYNLEE----LEKKAEEYEKLKEKLI 535
                         170       180
                  ....*....|....*....|....
gi 2024499903 474 QMAATIKQLEQRSHLELELKRERE 497
Cdd:PRK03918  536 KLKGEIKSLKKELEKLEELKKKLA 559
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
108-263 4.88e-101

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 304.23  E-value: 4.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17696     1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17696    81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
108-263 1.03e-98

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 298.05  E-value: 1.03e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17695     1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17695    81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
108-262 5.94e-97

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called 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 homolog 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 called 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. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 293.32  E-value: 5.94e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17681     1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17681    81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
108-263 7.18e-94

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called 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 homolog 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; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 285.65  E-value: 7.18e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 108 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 187
Cdd:cd17694     1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17694    81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
143-266 2.56e-46

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 426965  Cd Length: 136  Bit Score: 159.78  E-value: 2.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 143 QFFVVMEHCLKHGLKAKKT-----------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLAL 211
Cdd:pfam02759   1 SLCAALEALLSHGLKRKALsaslsliegyyGLLPERSFWDLLERVGKLVPPAEELLSSVQALEQIHTSDGRGRAWIRLAL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 212 MQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 266
Cdd:pfam02759  81 NEKLLEQWLNLLLSNKELLSKYYEPWALLRDPEFVeILLGLLVGLSALDFNLCLDL 136
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
111-262 2.28e-36

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 133.29  E-value: 2.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 111 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 188
Cdd:cd17684     1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 189 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17684    77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
119-262 1.55e-33

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 125.62  E-value: 1.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 119 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 189
Cdd:cd17671     2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANF 262
Cdd:cd17671    81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
111-263 4.03e-26

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 104.28  E-value: 4.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 111 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 188
Cdd:cd17700     1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 189 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17700    77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
111-263 1.61e-23

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 97.02  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 111 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 187
Cdd:cd17699     1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 188 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 263
Cdd:cd17699    76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
570-619 7.93e-22

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 88.63  E-value: 7.93e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499903 570 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSI-NPERVCNPCH 619
Cdd:cd15744     1 SCSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
566-619 3.68e-20

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: 84.36  E-value: 3.68e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 566 GNAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCH 619
Cdd:cd15721     5 KEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN smart00593
domain involved in Ras-like GTPase signaling;
203-265 2.04e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 79.19  E-value: 2.04e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499903  203 GRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 265
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
120-259 7.45e-18

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439044  Cd Length: 150  Bit Score: 80.73  E-value: 7.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 120 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 194
Cdd:cd17682     2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 195 GLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIIAGLLVGLNVID 259
Cdd:cd17682    82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
567-629 8.43e-18

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 77.76  E-value: 8.43e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 567 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQQYSTS 629
Cdd:cd15759     9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
568-627 9.67e-18

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: 77.80  E-value: 9.67e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQQYS 627
Cdd:cd15758    12 ATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
109-255 5.22e-14

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 70.31  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 109 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 176
Cdd:cd17679     1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 177 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGL 255
Cdd:cd17679    81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
193-258 1.62e-12

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 65.71  E-value: 1.62e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 193 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMM-EEEGAIIAGLLVGLNVI 258
Cdd:cd17689    93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
571-619 3.39e-12

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: 61.39  E-value: 3.39e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCH 619
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSgkPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
568-622 1.41e-11

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: 60.14  E-value: 1.41e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903  568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN--PERVCNPCHKQL 622
Cdd:smart00064  10 VSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIerPVRVCDDCYENL 66
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
148-258 3.72e-11

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. 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; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 61.35  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 148 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRK 227
Cdd:cd17697    35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024499903 228 DLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVI 258
Cdd:cd17697   115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
119-240 5.02e-11

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 61.10  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 119 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 198
Cdd:cd17680    12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024499903 199 PVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALM 240
Cdd:cd17680    81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
568-622 5.08e-11

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 58.18  E-value: 5.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQL 622
Cdd:cd15730     9 VQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
149-259 5.13e-11

RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.


Pssm-ID: 439049  Cd Length: 161  Bit Score: 61.53  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 149 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 208
Cdd:cd17687    31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499903 209 LALMQKKLSEYMKALINRKdllSEFYEPNALMME-EEGAIIAGLLVGLNVID 259
Cdd:cd17687   110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
567-619 9.98e-11

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 57.54  E-value: 9.98e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 567 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLP--SSINPERVCNPCH 619
Cdd:cd15735     5 DSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
568-622 1.38e-10

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: 57.39  E-value: 1.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCHKQL 622
Cdd:pfam01363   9 ATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
571-618 2.08e-10

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: 56.58  E-value: 2.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI--NPERVCNPC 618
Cdd:cd15731    14 CMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
154-263 4.17e-10

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 59.33  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 154 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 225
Cdd:cd17677    65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024499903 226 RKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17677   140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
114-262 4.20e-10

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.


Pssm-ID: 439060  Cd Length: 158  Bit Score: 58.55  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 114 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPL-ELVEKlVPEAAE 185
Cdd:cd17698     2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFcECLAK-VKGLND 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499903 186 ITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEP-NALMMEEEGAIIAGLLVGLNviDANF 262
Cdd:cd17698    81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPrSVFLNHKYSSDIINSLYDLN--EVQF 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
283-500 7.27e-10

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: 62.38  E-value: 7.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  283 KDGNSTKGSegDGQITAILDQKNYVEELNRH---LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE 359
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  360 SSYILESNRKVTKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDD 439
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903  440 LRALKHELSFKLQSS--DMGVKQKS--ELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWS 500
Cdd:TIGR02168  815 LNEEAANLRERLESLerRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
571-622 7.51e-10

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 55.09  E-value: 7.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPE-RVCNPCHKQL 622
Cdd:cd15720     8 CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKfGIEKEvRVCDPCYEKL 61
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
571-619 1.75e-09

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: 53.97  E-value: 1.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPCH 619
Cdd:cd15733    10 CFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
568-618 3.06e-09

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 53.36  E-value: 3.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPC 618
Cdd:cd15732     8 AASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
568-622 3.95e-09

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 53.16  E-value: 3.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS--SINPERVCNPCHKQL 622
Cdd:cd15719     9 GDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-498 5.25e-09

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: 59.30  E-value: 5.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  304 KNYVEELNRHLSAtVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTE 383
Cdd:TIGR02168  263 QELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  384 ARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSE 463
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024499903  464 LNSRLEEK--TNQMAATIKQLEQRSHLELELKRERER 498
Cdd:TIGR02168  422 EIEELLKKleEAELKELQAELEELEEELEELQEELER 458
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
128-261 5.53e-09

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 55.35  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 128 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGR 204
Cdd:cd17686     6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 205 AWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAiiAGLLVGLNVIDAN 261
Cdd:cd17686    85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
571-618 7.05e-09

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 52.33  E-value: 7.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSS--INPERVCNPC 618
Cdd:cd15734    11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
291-497 7.53e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.96  E-value: 7.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKV 370
Cdd:COG1196    719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  371 TKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFK 450
Cdd:COG1196    799 EEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDE 878
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024499903  451 LQSSdmgVKQKSELNSRLEEKTNQMAATIKQLE-QRSHLELELKRERE 497
Cdd:COG1196    879 LKEL---EEEKEELEEELRELESELAELKEEIEkLRERLEELEAKLER 923
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
570-618 1.79e-08

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: 50.96  E-value: 1.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499903 570 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINP--ERVCNPC 618
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
571-624 1.95e-08

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 51.19  E-value: 1.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPCHKQLIQ 624
Cdd:cd15739    13 CPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
568-618 2.04e-08

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 50.84  E-value: 2.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLP--SSINPERVCNPC 618
Cdd:cd15727    10 CPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
190-263 2.88e-08

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053  Cd Length: 206  Bit Score: 54.29  E-value: 2.88e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17691   127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
307-502 3.48e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 56.65  E-value: 3.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  307 VEELNRHLSATVNNLQAKVDALEKSNTKLT---EELAVANNRIITLQEEMERVKEEssyiLESNRKVTKDRTADGQALTE 383
Cdd:COG1196    711 LEELERQLEELKRELAALEEELEQLQSRLEeleEELEELEEELEELQERLEELEEE----LESLEEALAKLKEEIEELEE 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  384 ARKQLKEEtqlRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDmgvKQKSE 463
Cdd:COG1196    787 KRQALQEE---LEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELE---KELEE 860
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024499903  464 LNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWSHS 502
Cdd:COG1196    861 LKEELEELEAEKEELEDELKELEEEKEELEEELRELESE 899
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
571-619 1.39e-07

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: 48.45  E-value: 1.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI---NPERVCNPCH 619
Cdd:cd15760     8 CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
317-509 1.49e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 430825 [Multi-domain]  Cd Length: 305  Bit Score: 53.59  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRkvtkdrtadgQALTEARKQLKEETQLRL 396
Cdd:pfam09787  41 GSTALSLELDELRQERDLLREELQQLNQQIEQLRTELQELEAQQQEEAESSR----------EQLQDLEEQLATERQARR 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 397 DVEKELEaqigmRQEMELamKMLEKDVCEKQDALVA-LRQQLDDLRALKHELSFKLQSSdmgvKQKSELNSRLEEKTNQM 475
Cdd:pfam09787 111 EAEAELE-----RLQEEL--RYLEEELRRTKATLQSrIKDREAEIEKLRNQLTNKSQSS----SSQSELENRLHQLTESL 179
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024499903 476 AATIKQLE----QRSHLELELKReRERWSHSHQSSQGN 509
Cdd:pfam09787 180 IQKQTMLEalstEKNSLVLQLER-LEQQIKELQGEASN 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
291-498 6.58e-07

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: 52.75  E-value: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnRKV 370
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-------ESL 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  371 TKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSfk 450
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE-- 907
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024499903  451 lqssdmgvKQKSELNSRLEEKTNQMAATIKQLEQrshLELELKRERER 498
Cdd:TIGR02168  908 --------SKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQER 944
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
312-498 6.64e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.79  E-value: 6.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  312 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRtadgQALTEARKQLKEE 391
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEI----EELEGEISLLRER 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  392 TQLRLDVEKELEAQIGMRQEmelAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQssdmgvKQKSELNSRLEEK 471
Cdd:COG1196    311 LEELENELEELEERLEELKE---KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLS------ALLEELEELFEAL 381
                          170       180
                   ....*....|....*....|....*..
gi 2024499903  472 TNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG1196    382 REELAELEAELAEIRNELEELKREIES 408
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
298-470 1.04e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.02  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  298 TAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTAD 377
Cdd:COG1196    351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKEL 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  378 GQALTEARKQLKEETQLRLDVEKELEAQIGMRQEmelamkmLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMG 457
Cdd:COG1196    431 EAELEELQTELEELNEELEELEEQLEELRDRLKE-------LERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGV 503
                          170
                   ....*....|...
gi 2024499903  458 VKQKSELNSRLEE 470
Cdd:COG1196    504 RAVLEALESGLPG 516
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
571-618 1.43e-06

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: 45.63  E-value: 1.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPERVCNPC 618
Cdd:cd15726    10 CLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
568-622 1.47e-06

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, 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: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 45.80  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 568 AQICQLCQE-ESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 622
Cdd:cd15755     8 ATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
568-619 1.95e-06

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: 45.43  E-value: 1.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 568 AQICQLCQE-ESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCH 619
Cdd:cd15717     8 APVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
120-254 2.05e-06

RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. This model contains the RUN domain of SGSM1.


Pssm-ID: 439065  Cd Length: 177  Bit Score: 48.47  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 120 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 179
Cdd:cd17703     3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 180 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALINRKdllSEFYEPNALMMEE-EGAIIAGLLVG 254
Cdd:cd17703    82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLVENS---SKYYEKEALLMDPvDGPILASLLVG 157
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
571-619 2.41e-06

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack 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. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 44.80  E-value: 2.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499903 571 CQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPCH 619
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKGNqKQKVCKQCH 51
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
291-497 2.77e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.48  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKV 370
Cdd:COG1196    747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  371 TKDRTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELsfk 450
Cdd:COG1196    827 EQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL--- 903
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024499903  451 lqssdmgvkqkSELNSRLEEKTNQMAATIKQLE-QRSHLELELKRERE 497
Cdd:COG1196    904 -----------KEEIEKLRERLEELEAKLERLEvELPELEEELEEEYE 940
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
299-498 3.59e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 50.14  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 299 AILDQKNYVEEL-NRHLSATVNNLQAKVDALEKSNTKLTEELAvANNRIITLQEEMERVKEESSYIlESNRKVTKDRTAD 377
Cdd:COG0419   534 KLEKLENLLEELeELKEKLQLQQLKEELRQLEDRLQELKELLE-ELRLLRTRKEELEELRERLKEL-KKKLKELEERLSQ 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 378 GQALTEARKQLKEETQLRlDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMG 457
Cdd:COG0419   612 LEELLQSLELSEAENELE-EAEEELESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEEL 690
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2024499903 458 VKQKSEL---NSRLEEKTNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG0419   691 EQLEEELeqlREELEELLKKLGEIEQLIEELESRKAELEELKKE 734
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-500 4.39e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.10  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  308 EELNRHLSATVNNL---QAKVDALEKSNTKLTEELAVANnRIITLQEEMERVkeESSYILESNRKVTKDRTADGQALTEA 384
Cdd:COG1196    175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELREL--ELALLLAKLKELRKELEELEEELSRL 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  385 RKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQssdmgvkqksEL 464
Cdd:COG1196    252 EEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELE----------EL 321
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024499903  465 NSRLEEKTNQMAATIKQLEQRSHLELELKRERERWS 500
Cdd:COG1196    322 EERLEELKEKIEALKEELEERETLLEELEQLLAELE 357
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
560-618 5.47e-06

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 43.95  E-value: 5.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024499903 560 EQPSGPGNaqICQLCQEESSRSKKKNICKNCGGIFCEACSANELP-LPSSIN-PERVCNPC 618
Cdd:cd15728     1 EPPWADGD--YCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPiIKFDLNkPVRVCDVC 59
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
296-498 5.76e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 49.71  E-value: 5.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  296 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRT 375
Cdd:COG1196    675 ELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  376 ADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSD 455
Cdd:COG1196    755 ELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELE 834
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2024499903  456 mgvKQKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG1196    835 ---EEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEE 874
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
565-619 7.98e-06

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 43.47  E-value: 7.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 565 PGNAQICQlCQEESSRSKKKNICKNCGGIFCEACSANELPLPS--SINPERVCNPCH 619
Cdd:cd15738     6 FRNVTECS-CSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
570-622 9.07e-06

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, 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.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 43.41  E-value: 9.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 570 ICQLC-QEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 622
Cdd:cd15754    10 ICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
312-580 1.13e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  312 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYI---LESNRKVTKDRTADGQALTEARKQL 388
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  389 KEE--------TQLRLD-VEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELsfKLQSSDMGvK 459
Cdd:TIGR02169  778 EEAlndlearlSHSRIPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIE-K 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  460 QKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERwSHSHQSSQGNKKGPKNWLKPDGKLRIQDENAKLkQAPREE 539
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRELERKIEELEAQIEKKRKRLSELKAKL-EALEEE 932
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2024499903  540 NSvlphKYGRKLQSSTQEEQEQPSGPGNAQICQLCQEESSR 580
Cdd:TIGR02169  933 LS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
570-618 1.14e-05

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 43.19  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024499903 570 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPC 618
Cdd:cd15743    11 MCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKNkSARVCDEC 60
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
314-498 1.89e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.79  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  314 LSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKEETQ 393
Cdd:COG1196    272 LKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQ 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  394 LRLDVEKELEAQigmRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELN-------- 465
Cdd:COG1196    352 LLAELEEAKEEL---EEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLedlkeelk 428
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903  466 --------------------SRLEEKTNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG1196    429 eleaeleelqteleelneelEELEEQLEELRDRLKELERELAELQEELQRLEK 481
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
568-622 1.90e-05

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: 42.73  E-value: 1.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 568 AQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPE-RVCNPCHKQL 622
Cdd:cd15729    13 APNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDNKEaRVCVPCYQTL 68
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
300-497 2.54e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  300 ILDQK--NYVEELnRHLSATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSyileSNRKVTKDRTAD 377
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVS----RIEARLREIEQK 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  378 GQALTEARKQLKEETQLRLDVEKELEAQIGM-RQEMELAMKMLEK---DVCEKQDALVALRQQLDDLRALKHELSFKLQS 453
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERDELEAQLRE 900
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024499903  454 SDMGVKQKSELNSRLEEKTNQMAATIKQLEQR-SHLELELKRERE 497
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEE 945
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-498 2.74e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 47.46  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  318 VNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMeRVKEESSYILESNRKVTKDRTAD-GQALTEARKQLKEETQLRL 396
Cdd:pfam01576  105 IQDLEEQLEEEEAARQKLQLEKVTTEAKIKKMEEDI-LLLEDQNNKLQKERKLLEERISEfTSNLAEEEEKSKSLNKLKN 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  397 -------DVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSsdmgvkqkseLNSRLE 469
Cdd:pfam01576  184 kheamisDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAKKEEELQA----------ALARLE 253
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024499903  470 EKTNQMAATIKQL-EQRSHL-ELELKRERER 498
Cdd:pfam01576  254 EETAQKNAALKKLrELEAQLsELQEDLESER 284
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
190-263 2.94e-05

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052  Cd Length: 209  Bit Score: 45.39  E-value: 2.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 190 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLNVIDAnFC 263
Cdd:cd17690   130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
305-508 4.38e-05

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 46.35  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 305 NYVEELNRHLSATVNNLQAKVDaLEKSNTKLTEELAvANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEA 384
Cdd:COG4487     2 KEIKVPIQTKPFTIPKCEDSIK-GEQARYKQIEQED-QSRILNTLEEFEKEANEKRAQYRSAKKKELSQLEEQLINQKKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 385 RKQLKEET--QLRLDVEKE---LEAQIGMRQEMELAMKMLEKDVCEKQDALVAL-----------RQQLDDLRALKHELS 448
Cdd:COG4487    80 QKNLFNEQikQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 449 FKLQSSDMGVKQKSElnSRLEEKTNQMaATIKQLEQRSHLELELKRERERWSHSHQSSQG 508
Cdd:COG4487   160 KKLEESLELEREKFE--EQLHEANLDL-EFKENEEQRESKWAILKKLKRRAELGSQQVQG 216
flhF PRK06995
flagellar biosynthesis protein FlhF;
4-128 6.40e-05

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 45.73  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903   4 AERAPLLPPPAESSRDGM-AAETPPGMERRAEPGPEEAAVTEEEDEARPASPPFFLLYPGHGGAAAPHGAWRPPAPRGGA 82
Cdd:PRK06995   61 AAQPPPAAAPAAVSRPAApAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAP 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2024499903  83 ALPVLLLSYPGPDGASAHPNYLMANERMnlmnMAKL-SIKGLIESAL 128
Cdd:PRK06995  141 RPRVPADAAAAVADAVKARIERIVNDTV----MQELrSLRGMLEEQL 183
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
567-620 7.12e-05

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: 40.77  E-value: 7.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024499903 567 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSINPE--RVCNPCHK 620
Cdd:cd15725     7 SCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
352-489 7.98e-05

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: 45.88  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 352 EMERVKEES---SYILESNRKVTKDRTADGQAL-TEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQ 427
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 428 DALV--ALRQQLDDLRALKHELSFKLQSSDMgVKQKSELNSRLE--EKTNQMAATIKQLE-QRSHLE 489
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQEQ-MRKATEERSRLEamEREREMMRQIVESEkARAEYE 592
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
567-622 9.60e-05

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 40.69  E-value: 9.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903 567 NAQICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCHKQL 622
Cdd:cd15742     8 HVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPLKYlKDRPAKVCDGCFAEL 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-497 9.65e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 317 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKVTKDRTADGQALTEA-RKQLKEETQLR 395
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA----IEELKKAKGKCPVCGRELTEEhRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 396 L-DVEKELEAQIGMRQEMELAMKMLEKdVCEKQDALVALRQQLDDLRALKHELS-FKLQSsdmgVKQKSELNSRLEEKTN 473
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKkYNLEE----LEKKAEEYEKLKEKLI 535
                         170       180
                  ....*....|....*....|....
gi 2024499903 474 QMAATIKQLEQRSHLELELKRERE 497
Cdd:PRK03918  536 KLKGEIKSLKKELEKLEELKKKLA 559
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
296-507 1.63e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 44.63  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 296 QITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnrKVTKDRT 375
Cdd:COG4372    82 QLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQA--------QDLQTRL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 376 ADgqaLTEARKQLKEETQLRLDVEKELEAQIGM----RQEMELAMKMLE---KDVCEKQDALVALRQQLDDLRALKHELS 448
Cdd:COG4372   154 KT---LAEQRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQTA 230
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024499903 449 FKLQSSDmgvKQKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWSHSHQSSQ 507
Cdd:COG4372   231 QAIQQRD---AQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYV 286
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
285-501 1.85e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 44.71  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  285 GNSTKGSEGDGQITAILDQKNYVEELNRH-----------LSATVNNLQA-----------KVDALEK----SNTKLTE- 337
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdLESTVSQLRSelreakrmyedKIEELEKqlvlANSELTEa 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  338 ---------ELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLKE---ETQLRLDVEKELEAQ 405
Cdd:pfam15921  362 rterdqfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSE 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  406 IGMRQEMELAMKMLEKDVCEKQDALVA-LRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKTNQMAAT---IKQ 481
Cdd:pfam15921  442 CQGQMERQMAAIQGKNESLEKVSSLTAqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATnaeITK 521
                          250       260
                   ....*....|....*....|....
gi 2024499903  482 LEQRSHLELE----LKRERERWSH 501
Cdd:pfam15921  522 LRSRVDLKLQelqhLKNEGDHLRN 545
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
307-485 2.28e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 307 VEELNRHLSATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKVTKDR 374
Cdd:PRK04778  280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQL 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 375 TADGQALTEARKQLKEETQLRLDVEKELEaqigmrqEMELAMKMLEKDVCEKQDALVAL-------RQQLDDLRALKHEL 447
Cdd:PRK04778  358 ESLEKQYDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNKLHEI 430
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024499903 448 SFKLQSSDM-GVKQksELNSRLEEKTNQMAATIKQLEQR 485
Cdd:PRK04778  431 KRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
323-485 2.65e-04

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 43.90  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 323 AKVDALEKSNTkLTEELAVANNRIITLQEEMERVKEesSYILESN-----RKVTKDRTADGQALTEARKQLKEETQLRLD 397
Cdd:COG4477   303 AKNVVEENLPI-LPDYLEKAKENNEHLKEEIERVKE--SYRLAETelgsvRKFEKELKELESVLDEILENIEAQEVAYSE 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 398 VEKELEaqigmrqEMELAMKMLEKDVCEKQDALVALR-------QQLDDLRALKHELSFKLQSSDM-GVKQksELNSRLE 469
Cdd:COG4477   380 LQDNLE-------EIEKALTDIEDEQEKVQEHLTSLRkdelearENLERLKSKLHEIKRYMEKSNLpGLPE--TFLSLFF 450
                         170
                  ....*....|....*.
gi 2024499903 470 EKTNQMAATIKQLEQR 485
Cdd:COG4477   451 TAGHEIQDLMKELSEV 466
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
283-447 2.86e-04

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 43.17  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 283 KDGNSTKGSEGDGQITAILDQK----NYVEELNRHLSAT---VNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEM-E 354
Cdd:COG3883    26 AALLSDKIQNQDSKLSELQKEKkniqNEIESLDNQIEEIqskIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLkK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 355 RVK------EESSY----------------------ILESNRKVTKDRTADGQALTEARKQLkeetqlrldvEKELEAQI 406
Cdd:COG3883   106 RARamqvngTATSYidvilnsksfsdlisrvtaisvIVDADKKILEQQKEDKKSLEEKQAAL----------EDKLETLV 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2024499903 407 GMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHEL 447
Cdd:COG3883   176 ALQNELETQLNSLNSQKAEKNALIAALAAKEASALGEKAAL 216
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
313-474 2.86e-04

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 42.74  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 313 HLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYiLESNRKVTKDRTADGQALTEARKQLKEET 392
Cdd:COG1579    14 KLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQ-LESEIQEIRERIKRAEEKLSAVKDERELR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 393 QLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDMGVKQKSELNSRLEEKT 472
Cdd:COG1579    93 ALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEKL 172

                  ..
gi 2024499903 473 NQ 474
Cdd:COG1579   173 DP 174
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
569-618 3.56e-04

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 38.83  E-value: 3.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024499903 569 QICQLCQEE-SSRSKKKNICKNCGGIFCEACSANElplPSSINPERVCNPC 618
Cdd:cd15740     6 QTCKGCNESfNSITKRRHHCKQCGAVICGKCSEFK---DLASRHNRVCRDC 53
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
570-618 3.85e-04

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). 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. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275  Cd Length: 56  Bit Score: 38.70  E-value: 3.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 570 ICQLCQEESSRSKKKNICKNCGGIFCEACSANELPLPSSI------NPERVCNPC 618
Cdd:cd15736     1 CCHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAydprngKWYRCCHSC 55
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
578-622 6.18e-04

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin 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. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 38.25  E-value: 6.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 578 SSRSKKKNICKNCGGIFCEACSANELP--LPSSINPE------RVCNPCHKQL 622
Cdd:cd15723    10 SVLLKKRRSCNNCGNAFCSRCCSKKVPrsVMGATAPAaqretvFVCSGCNDKL 62
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
308-534 6.32e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 308 EELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQ 387
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 388 LKE-ETQLrLDVEKELEAQIgmrqemelaMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSSDmgvKQKSELNS 466
Cdd:TIGR04523 290 LNQlKSEI-SDLNNQKEQDW---------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK---KELTNSES 356
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024499903 467 RLEEKTNQMAATIKQLEQrshleleLKRERERWSHSHQSSQGNKKGPKNwlkpdgKLRIQDENAKLKQ 534
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEK-------LKKENQSYKQEIKNLESQINDLES------KIQNQEKLNQQKD 411
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
309-510 6.56e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 42.79  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 309 ELNRHLSATVNNLQAKVD---ALEKSNTKLTEELAVANNriiTLQEEMERVKEESSYILESNRKVtKDRTadgQALTEAR 385
Cdd:pfam05557  31 ELERKASALARQLERESDrnqELQKRIRLLEKREAEAEE---ALREQAELNRLKKKNLEALNKKL-NEKE---SQLADAR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 386 kqlkeETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVcekqdalvaLRQQLDDLRALKHELSFKLQSSDMGVKQKSELN 465
Cdd:pfam05557 104 -----EVISCLKNELSELRRQIQRQELELSSTNSELEE---------LQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAE 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 466 SRLEE------KTNQMAATIK----QLEQRSHLELELKRERERWSHsHQSSQGNK 510
Cdd:pfam05557 170 QRIKElefeiqSQEQDSEIVKnsksELARIPELERELERLREHNKH-LNENIENK 223
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
304-492 8.53e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 42.45  E-value: 8.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  304 KNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAvannriiTLQEEMERVKEESSYILESNRKVTKDRTADGQALTE 383
Cdd:pfam01576  400 KQDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLS-------KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  384 ARKQLKEETQLRLDVEKELEAqigMRQEMELAMKMLEKDVCEKQDA---LVALRQQLDDLRALKHELSFKLQSSDMGVKQ 460
Cdd:pfam01576  473 TQELLQEETRQKLNLSSRLRQ---LEDEKNSLQEQLEEEEEAKRNVerqLQTLQAQLSDLKKKLEEDAGAVEALEEGRKR 549
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024499903  461 KSE----LNSRLEEKTnqmAATIKQLEQRSHLELEL 492
Cdd:pfam01576  550 LQReleaLTQRLEEKA---AAYDKLEKTKNRLQQEL 582
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
299-498 1.06e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.05  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 299 AILDQKNYVEELNRHLSATVNNLQAKVDALEKS-------NTKLTEELAVANNRIITLQEEMERVKEE------SSYILE 365
Cdd:COG0419   484 EELEEELSREKEEAELREEIEELEKELRELEEEliellelEEALKEELEEKLEKLENLLEELEELKEKlqlqqlKEELRQ 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 366 SNRKVTKDRTADgQALTEARKQLKEETQLRlDVEKELEAQIGMRQEMELAMKMLEKDvCEKQDALVALRQQLDDLRALKH 445
Cdd:COG0419   564 LEDRLQELKELL-EELRLLRTRKEELEELR-ERLKELKKKLKELEERLSQLEELLQS-LELSEAENELEEAEEELESELE 640
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 446 ELSFKLQSSDMGVKQKSELNSRLEEKTNQmaatIKQLEQRSHLELELKRERER 498
Cdd:COG0419   641 KLNLQAELEELLQAALEELEEKVEELEAE----IRRELQRIENEEQLEEKLEE 689
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
282-497 1.07e-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: 42.03  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 282 LKDGNSTKGSEGDGQITAILDQKNYVEELNRHLSATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 354
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 355 RVKEEssyiLESNRKVtkdRTADGQALTEARKQLKEETQLRLDVEKELEAQIG-MRQEMELAMKMLEKDVCEKQDALVAL 433
Cdd:pfam17380 393 RVRQE----LEAARKV---KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrLEEERAREMERVRLEEQERQQQVERL 465
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 434 RQQLDDLRALKHElsfklqssdmgvKQKSELNSRLEEKTNQMAATiKQLEQRSHLELELKRERE 497
Cdd:pfam17380 466 RQQEEERKRKKLE------------LEKEKRDRKRAEEQRRKILE-KELEERKQAMIEEERKRK 516
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-99 1.48e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903   2 AEAERAPLLPPPAESSRDGMAAETPPGMERRAEPGPEEAAVTEEEDEARPASPPffllYPGHGGAAAPHGAWRPPA--PR 79
Cdd:PRK12323  395 AAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP----APAPAPAAAPAAAARPAAagPR 470
                          90       100
                  ....*....|....*....|
gi 2024499903  80 GGAALPVLLLSYPGPDGASA 99
Cdd:PRK12323  471 PVAAAAAAAPARAAPAAAPA 490
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
296-561 1.57e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  296 QITAILDQknyvEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIItLQEEMERVKEESSyilesnRKVTKDRT 375
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAI------TCTAQCEK 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  376 ADGQALTEARKQLKEETQLRLDVEK--ELEAQIG-MRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQ 452
Cdd:TIGR00618  456 LEKIHLQESAQSLKEREQQLQTKEQihLQETRKKaVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  453 SSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERERWSHSHQSSQGNKKGPKNWLKPDGKLRIQdeNAKL 532
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM--LACE 613
                          250       260
                   ....*....|....*....|....*....
gi 2024499903  533 KQAPREENSVLPHKYgRKLQSSTQEEQEQ 561
Cdd:TIGR00618  614 QHALLRKLQPEQDLQ-DVRLHLQQCSQEL 641
PRK11281 PRK11281
mechanosensitive channel MscK;
312-507 2.00e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  312 RHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE----SSYILESNRKVTKDRTADGQALTEARKQ 387
Cdd:PRK11281   117 TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyanSQRLQQIRNLLKGGKVGGKALRPSQRVL 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  388 LKEETQLrldvekeLEAQIGMRQEmELAMKMLEKDVCEKQDALVALRQQLddlraLKHELSFkLQSSdmgVKQKselnsR 467
Cdd:PRK11281   197 LQAEQAL-------LNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQR-----LEHQLQL-LQEA---INSK-----R 254
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2024499903  468 LE--EKTNQMAATIKQLEQRSHLELeLKRERErwsHSHQSSQ 507
Cdd:PRK11281   255 LTlsEKTVQEAQSQDEAARIQANPL-VAQELE---INLQLSQ 292
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1-99 2.50e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903   1 MAEAERAPLLPPPAESSRDGMAAETPPGMERRAEPGPEEAAVTEEEDEARPASPP----FFLLYPGHGGAAAPHGAWRPP 76
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPpspaGNAPAGGAPSPPPAAAPSAQP 466
                          90       100
                  ....*....|....*....|...
gi 2024499903  77 APRGGAALPVLLLSYPGPDGASA 99
Cdd:PRK07764  467 APAPAAAPEPTAAPAPAPPAAPA 489
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
379-498 3.21e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.85  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  379 QALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLRALKHELSFKLQSsdmGV 458
Cdd:COG1196    674 EELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEE---LE 750
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2024499903  459 KQKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG1196    751 EELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQA 790
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
568-619 3.87e-03

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 35.95  E-value: 3.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024499903 568 AQICQLCQEES-SRSKKKNICKNCGGIFCEACSANELPLPS-SINPERVCNPCH 619
Cdd:cd15724     7 VSVCMVCQVERfSMFNRRHHCRRCGRVVCSSCSTKKMLVEGyRENPVRVCDQCY 60
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
570-622 3.91e-03

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 36.31  E-value: 3.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024499903 570 ICQLCQEE-SSRSKKKNICKNCGGIFCEACSANELPLPSSIN-PERVCNPCHKQL 622
Cdd:cd15741    11 MCMRCKEPfNALTRRRHHCRACGYVVCWKCSDYKATLEYDGNkLNRVCKHCYVIL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
291-495 4.02e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  291 SEGDGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYiLESNRKV 370
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIAS-LERSIAE 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903  371 TKDRTADGQA-----LTEARKQLKEETQLRLDVE---KELEAQIGMRQEMELAMKMLEKDVCEKQDALVALRQQLDDLR- 441
Cdd:TIGR02169  313 KERELEDAEErlaklEAEIDKLLAEIEELEREIEeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRe 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024499903  442 ---ALKHELSFKLQSSDMGVKQKSELNSRLEEktnqMAATIKQLEQRsHLELELKRE 495
Cdd:TIGR02169  393 kleKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAK-INELEEEKE 444
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
324-511 4.45e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 324 KVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyILESNRKVTKDrtadgqaLTEARKQLKEETQLRLDVeKELE 403
Cdd:TIGR04523  97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ---KKENKKNIDKF-------LTEIKKKEKELEKLNNKY-NDLK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 404 AQIgmrQEMELAMKMLEKDVCEKQDALVALRQQlddLRALKHELSfKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLE 483
Cdd:TIGR04523 166 KQK---EELENELNLLEKEKLNIQKNIDKIKNK---LLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
                         170       180
                  ....*....|....*....|....*....
gi 2024499903 484 QR-SHLELELKRERERWSHSHQSSQGNKK 511
Cdd:TIGR04523 239 QEiNEKTTEISNTQTQLNQLKDEQNKIKK 267
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
328-484 5.35e-03

Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 39.97  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 328 LEKSNTKLTEELAVANNRIIT-LQEEMERVKEESSYILESNRKVTKdrtadgqaLTEARKQLKEETQ-LRLDVEKELEAQ 405
Cdd:COG5185   247 LEDNYEPSEQELKLGFEKFVHiINTDIANLKTQNDNLYEKIQEAMK--------ISQKIKTLREKWRaLKSDSNKYENYV 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 406 IGMRQEMEL---AMKMLEKDVCEKQDALVALRQQLDDLRAL--KHELS---FKLQSS---------DMGVKQKSELNSRL 468
Cdd:COG5185   319 NAMKQKSQEwpgKLEKLKSEIELKEEEIKALQSNIDELHKQlrKQGISteqFELMNQerekltrelDKINIQSDKLTKSV 398
                         170
                  ....*....|....*.
gi 2024499903 469 EEKTNQMAATIKQLEQ 484
Cdd:COG5185   399 KSRKLEAQGIFKSLEK 414
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
294-498 5.37e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 39.74  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 294 DGQITAILDQKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKVtKD 373
Cdd:COG0419   231 EQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEEL-EG 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 374 RTADGQALTEARKQLKEETQLRLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDAL--------VALRQQLDDLRALKH 445
Cdd:COG0419   310 LRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELeerleeleKELEKALERLKQLEE 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024499903 446 ELSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQLEQRSHLELELKRERER 498
Cdd:COG0419   390 AIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQ 442
46 PHA02562
endonuclease subunit; Provisional
303-481 5.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 303 QKNYVEELNRHLSATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMErvkeessyilesnrkvtkDRTADGQALT 382
Cdd:PHA02562  200 YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE------------------DPSAALNKLN 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 383 EARKQLKEETQLrldVEKEleaqigmrqemelaMKMLEK-DVC---------------EKQDALVALRQQLDDLRALKHE 446
Cdd:PHA02562  262 TAAAKIKSKIEQ---FQKV--------------IKMYEKgGVCptctqqisegpdritKIKDKLKELQHSLEKLDTAIDE 324
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024499903 447 LSFKLQSSDMGVKQKSELNSRLEEKTNQMAATIKQ 481
Cdd:PHA02562  325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
319-498 9.22e-03

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


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 38.93  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 319 NNLQAKVDALEKSNTKLTEELAvannriiTLQEEMERVKEESSYILESNRKVTKDRTADGQALTEARKQLK----EETQL 394
Cdd:COG4942    41 KQIQKEIAALEKKIREQQDQRA-------KLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNalevQEREQ 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024499903 395 RLDVEKELEAQIGMRQEMELAMKMLEKDVCEKQDALV-------ALRQQLDDLRALKHELsfKLQSSDMGVKQKSELNSR 467
Cdd:COG4942   114 RRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIyygalnpARAERIDALKATLKQL--AAVRAEIAAEQAELTTLL 191
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024499903 468 LEEKTNQMAATIKQLEQRS---HLELELKRERER 498
Cdd:COG4942   192 SEQRAQQAKLAQLLEERKKtlaQLNSELSADQKK 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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