NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|576795839|ref|NP_001276703|]
View 

protein RUFY3 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
118-273 1.35e-99

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: 301.53  E-value: 1.35e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.94e-19

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: 80.54  E-value: 6.94e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-554 7.56e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESS------YLLESNRKGPKQDRTAEGQALSEA 395
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeYELLAELARLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 396 RKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHElafKLQSSDLGVKQKSEL 475
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE---AEEELEELAEELLEA 391
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 476 NSRLEEKTNQMAATIKQLEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNR 554
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
118-273 1.35e-99

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: 301.53  E-value: 1.35e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-276 2.97e-43

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: 460679  Cd Length: 134  Bit Score: 152.04  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  153 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 223
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 576795839  224 KKLSEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 276
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.94e-19

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: 80.54  E-value: 6.94e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 6.66e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 78.04  E-value: 6.66e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-554 7.56e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESS------YLLESNRKGPKQDRTAEGQALSEA 395
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeYELLAELARLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 396 RKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHElafKLQSSDLGVKQKSEL 475
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE---AEEELEELAEELLEA 391
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 476 NSRLEEKTNQMAATIKQLEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNR 554
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
605-660 1.70e-09

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: 54.36  E-value: 1.70e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   605 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 660
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
609-660 2.87e-08

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: 50.84  E-value: 2.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839  609 QVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 660
Cdd:pfam01363  10 TVCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-554 3.35e-08

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: 56.99  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 529
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 576795839   530 EALTRQRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-548 8.17e-06

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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.40  E-value: 8.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:pfam01576  163 EFTSNLAEEeekakslSKLKNkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   460 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 538
Cdd:pfam01576  243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALKTELEdTLDTTAAQ 318
                          250
                   ....*....|
gi 576795839   539 LELELKQEKE 548
Cdd:pfam01576  319 QELRSKREQE 328
PRK11281 PRK11281
mechanosensitive channel MscK;
317-539 2.27e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  317 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 385
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  386 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 438
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  439 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELD 510
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 576795839  511 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 539
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
 
Name Accession Description Interval E-value
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
118-273 1.35e-99

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: 301.53  E-value: 1.35e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
118-273 1.27e-96

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: 293.81  E-value: 1.27e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17695   81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
118-272 6.86e-94

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: 286.77  E-value: 6.86e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17681    1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANF 272
Cdd:cd17681   81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
118-273 1.85e-90

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: 277.94  E-value: 1.85e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 118 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 197
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17694   81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-276 2.97e-43

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: 460679  Cd Length: 134  Bit Score: 152.04  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  153 QFFVVMEHCLKHGLKA------KKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKT---PVGRGRAWLRLALMQ 223
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 576795839  224 KKLSEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCMKG 276
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
121-272 1.45e-35

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: 131.37  E-value: 1.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 121 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLG--QNKSFWGPLELVEKLVPEAAeiTA 198
Cdd:cd17684    1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IA 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839 199 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANF 272
Cdd:cd17684   77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
129-272 1.67e-31

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: 119.84  E-value: 1.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 129 SIKGLIESALNLGR-------TLDSDYAPLQQFFVVMEHCLKHGLKAKKtFLGQNKSFWGPLELVEKLVPEAAEITA--S 199
Cdd:cd17671    2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKQAirD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839 200 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANF 272
Cdd:cd17671   81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRdPEEAELFLSLLVGLSSLDFNL 154
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
121-273 3.53e-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: 104.67  E-value: 3.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 121 NLMNMAKLSIKGLIESALNlgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQN--KSFWGPLELVEKLVPEAAeiTA 198
Cdd:cd17700    1 NLITVCRFSVKTLIDRSCF--ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFWDYIRVACSKVPHNC--IC 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 199 SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17700   77 SIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
121-273 1.28e-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: 97.40  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 121 NLMNMAKLSIKGLIESALnlGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQnKSFWGPLELVEKLVPEaaEIT 197
Cdd:cd17699    1 NLITVCRFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVPN--NCI 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 198 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFC 273
Cdd:cd17699   76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
611-657 6.94e-19

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: 80.54  E-value: 6.94e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDD---SLTKNTCRNCRGTFCNACTTNELPLPSSI-KPERVCNPCH 657
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 6.66e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 78.04  E-value: 6.66e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795839   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
611-657 3.53e-17

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: 75.88  E-value: 3.53e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCH 657
Cdd:cd15721   10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
130-269 9.46e-16

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: 74.95  E-value: 9.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 130 IKGLIESALNLGRTLDSDYAP-LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLE-LVEKLVPEA---AEITASVKDLP 204
Cdd:cd17682    2 LKGCVLDLKSEFGEITDPDNPyLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCK 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839 205 GLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEE-GAIIAGLLVGLNVID 269
Cdd:cd17682   82 KVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLNEIN 147
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
611-667 1.09e-14

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: 69.28  E-value: 1.09e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYSSS 667
Cdd:cd15759   13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
611-665 5.60e-14

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: 67.01  E-value: 5.60e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIKQYS 665
Cdd:cd15758   15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
119-265 9.62e-13

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: 66.85  E-value: 9.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 119 RMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAK-----KTFLGQN------KSFWGPLELV- 186
Cdd:cd17679    1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKfiskvSSVFSGDvdklpePNFWPLLLKFs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 187 EKlvpeaaEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGL 265
Cdd:cd17679   81 HR------DVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRdPEQLDILKSLLQGL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
203-268 3.61e-11

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: 61.86  E-value: 3.61e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 203 LPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVI 268
Cdd:cd17689   93 LKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRdEERSSMLPNMAAGLGSI 159
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
158-268 1.41e-10

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: 59.81  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 158 MEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKK 237
Cdd:cd17697   35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                         90       100       110
                 ....*....|....*....|....*....|..
gi 576795839 238 ELLSEFYEVNA-LMMEEEGAIIAGLLVGLNVI 268
Cdd:cd17697  115 ELTGEWYYARSpFLSPELRSDILDSLYELNGV 146
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-554 7.56e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESS------YLLESNRKGPKQDRTAEGQALSEA 395
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeYELLAELARLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 396 RKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHElafKLQSSDLGVKQKSEL 475
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE---AEEELEELAEELLEA 391
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 476 NSRLEEKTNQMAATIKQLEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNR 554
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
611-657 8.60e-10

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: 54.85  E-value: 8.60e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 657
Cdd:cd00065    2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
124-272 1.28e-09

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: 57.40  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 124 NMAKLSIKGLIESALNLGRTLDSDYAP-------LQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPL-ELVEKlVPEAAE 195
Cdd:cd17698    2 SQLQKIIRDLQDCVTELKKEFEETGEPitddsttLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFcECLAK-VKGLND 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576795839 196 ITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSE-FYEVNALMMEEEGAIIAGLLVGLNviDANF 272
Cdd:cd17698   81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDwYYPRSVFLNHKYSSDIINSLYDLN--EVQF 156
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
129-250 1.43e-09

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: 56.87  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 129 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKktflgqNKSFWGpleLVEKLVPEAAEItaSVKDLPGLKT 208
Cdd:cd17680   12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLRRG------NRGYWP---FVKEFTHKETIK--QIENLPNVTT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 576795839 209 PVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALM 250
Cdd:cd17680   81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALL 122
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
159-269 1.63e-09

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: 57.30  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 159 EHCLKHGLKAKK-TFLGQNKSFwGPLELVEKLVPEAAEITASVKDL------PGLKTPVGRGRA-------------WLR 218
Cdd:cd17687   31 DACLLHGLRKRAlGLFRSSSTF-SLLQKVAKSCPPAADILRKVQEIenlsenKRSSSSSGSNSSnshgnsssnrkilWIR 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576795839 219 LALMQKKLSEYMKALINKKellSEFYEVNALMME-EEGAIIAGLLVGLNVID 269
Cdd:cd17687  110 IALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
605-660 1.70e-09

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: 54.36  E-value: 1.70e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   605 SEKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCHEQL 660
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-554 2.30e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 306 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDR 385
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERR 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 386 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 465
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 466 DlgvKQKSELNSRLEEKTNQMAAtIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQ 545
Cdd:COG1196  392 L---RAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                 ....*....
gi 576795839 546 EKERKSQNR 554
Cdd:COG1196  468 LLEEAALLE 476
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
610-657 4.01e-09

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: 52.92  E-value: 4.01e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576795839 610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPCH 657
Cdd:cd15735    8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
611-656 6.78e-09

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: 52.40  E-value: 6.78e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 656
Cdd:cd15730   12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDAC 59
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
164-273 1.00e-08

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: 55.48  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 164 HGLKAKktflgQNKS-FWGPL----ELVEKLVPEAAEITA---SVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALIN 235
Cdd:cd17677   65 HGLQTK-----QGKSaLWSHLlayqENEERLKPLPESLLFdmkNVQNMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 576795839 236 KKELLSEFYEVNA-LMMEEEGAIIAGLLVGLNVIDAnFC 273
Cdd:cd17677  140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVDY-FC 177
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
610-660 1.61e-08

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: 51.23  E-value: 1.61e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 610 VCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS-SI-KPERVCNPCHEQL 660
Cdd:cd15720    7 ECHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIeKEVRVCDPCYEKL 61
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
609-660 2.87e-08

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: 50.84  E-value: 2.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839  609 QVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCHEQL 660
Cdd:pfam01363  10 TVCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKISLLPELgsnKPVRVCDACYDTL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-554 3.35e-08

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: 56.99  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRqsAELDNRLfkQDFGDKINSLQLEV 529
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*
gi 576795839   530 EALTRQRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELR 914
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
138-271 3.58e-08

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: 53.04  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 138 LNLGRTLD--SDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNkSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVG-RGR 214
Cdd:cd17686    6 LLLSRSSNvwSTYGGLQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGR 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 215 AWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAiiAGLLVGLNVIDAN 271
Cdd:cd17686   85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYA--TALLICLTAVELN 139
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
611-656 4.46e-08

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: 50.02  E-value: 4.46e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 656
Cdd:cd15734   11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
200-273 4.88e-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 [Multi-domain]  Cd Length: 206  Bit Score: 53.91  E-value: 4.88e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 200 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNA-LMMEEEGAIIAGLLVGLNVIDAnFC 273
Cdd:cd17691  127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVDY-FC 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-555 6.91e-08

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: 55.83  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   314 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 393
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-----------LKHELAFKL 462
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearlerLEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   463 Q-----SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFkQDFGDKINSLQLEVEALTRQRT 537
Cdd:TIGR02168  421 QeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499
                          250       260
                   ....*....|....*....|....
gi 576795839   538 QLE------LELKQEKERKSQNRG 555
Cdd:TIGR02168  500 NLEgfsegvKALLKNQSGLSGILG 523
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
611-660 1.58e-07

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: 48.54  E-value: 1.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCHEQL 660
Cdd:cd15719   12 CTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
619-656 3.01e-07

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: 47.59  E-value: 3.01e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 576795839 619 SLTKNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPC 656
Cdd:cd15732   21 ASRKHHCRNCGNVFCGSCCNQKLPVPSQqlFEPSRVCKSC 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-555 4.51e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 308 TAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQD 384
Cdd:COG1196  267 AELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 385 RTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAfklqs 464
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----- 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 465 sdlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERgRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELK 544
Cdd:COG1196  421 -----EELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
                        250
                 ....*....|.
gi 576795839 545 QEKERKSQNRG 555
Cdd:COG1196  495 LLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-551 4.92e-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: 53.14  E-value: 4.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 380
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   381 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 460
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   461 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRqaERGRQSAELDNRLfKQDFGDKINSLQLEVEALTRQRTQL- 539
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-ENKIEDDEEEARRRLKRLENKIKELg 985
                          250
                   ....*....|....*...
gi 576795839   540 ------ELELKQEKERKS 551
Cdd:TIGR02168  986 pvnlaaIEEYEELKERYD 1003
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
344-601 9.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 9.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 344 KLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEM 423
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 424 ELAMKmlekdvcEKQDALVSLRQQLDDLRALKHELAfklqssdlgvKQKSELNSRLEEKtnqmAATIKQLEQRLRQAERG 503
Cdd:COG1196  315 EERLE-------ELEEELAELEEELEELEEELEELE----------EELEEAEEELEEA----EAELAEAEEALLEAEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 504 RQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLElELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKK 583
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
                        250
                 ....*....|....*...
gi 576795839 584 PLEESHRLLTHPAEEQGQ 601
Cdd:COG1196  453 ELEEEEEALLELLAELLE 470
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
606-656 9.94e-07

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: 46.22  E-value: 9.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 606 EKPQVCQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLP--SSIKPERVCNPC 656
Cdd:cd15727    8 KECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-508 1.20e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 306 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyLLESNRKgpkqdR 385
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEA-----L 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 386 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 465
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 576795839 466 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE 508
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
622-656 1.25e-06

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: 46.18  E-value: 1.25e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSSI--KPERVCNPC 656
Cdd:cd15731   27 RHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
130-264 2.72e-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: 48.08  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 130 IKGLIESALNLgRTLDSDYAPLQQFFVVMEHCLKHGLKAKKT-FLGQNK----------SFWGPLELVEKL--------- 189
Cdd:cd17703    3 VKQIMEEAVTR-KFVHEDSSHIISFCAAVEACVLHGLKRRAAgFLRSNKiaalfmkvgkSFPPAEELCRKVqeleqllen 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 190 ----VPEAAEITASVKDLPGLkTPVGRGRAWLRLALMQKKLSEYMKALInkkELLSEFYEVNALMMEE-EGAIIAGLLVG 264
Cdd:cd17703   82 krnqMQGLQENVRKMPKLPNL-SPQAIKHLWIRTALFEKVLDKIVHYLV---ENSSKYYEKEALLMDPvDGPILASLLVG 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
359-579 2.82e-06

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: 50.84  E-value: 2.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   359 LQEEMERVKEESsYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQ 438
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   439 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 499
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   500 AERGRQSAELDNRLFK---QDFGDKINSLQLEVEALTRQRTQLELELKQEKERKsqnrgtpgKGAQKPELRMDGKHRIQE 576
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRL--------GDLKKERDELEAQLRELE 902

                   ...
gi 576795839   577 ENV 579
Cdd:TIGR02169  903 RKI 905
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
324-588 2.89e-06

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: 50.40  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEsSYLLESNRKGPK---QDRTAEGQALSEARKHLK 400
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE-IKNLESQINDLEskiQNQEKLNQQKDEQIKKLQ 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  401 EETQLrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSL-------RQQLDDL----RALKHELAFKLQSSDLGV 469
Cdd:TIGR04523 419 QEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntreslETQLKVLsrsiNKIKQNLEQKQKELKSKE 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  470 KQKSELN---SRLEEKTNQMAATIKQLEQRLRQ-----AERGRQSAELDNRLFKQDFG--------------DKINSLQL 527
Cdd:TIGR04523 496 KELKKLNeekKELEEKVKDLTKKISSLKEKIEKlesekKEKESKISDLEDELNKDDFElkkenlekeideknKEIEELKQ 575
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839  528 EVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGKHrIQEENVKL---KKPLEES 588
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQkEKEKKDLIKEIEEKEKKISSLEKELEK-AKKENEKLssiIKNIKSK 639
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
609-657 3.22e-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: 44.66  E-value: 3.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 609 QVCQLCQEddslTKNT-------CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 657
Cdd:cd15717    9 PVCMHCKK----TKFTainrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
305-560 4.46e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 305 GQITAILDQKNYVEELNRHLNAtvnnLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQD 384
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 385 RTAEGQALSEARKHLKEE--TQLRLDVEKELELQISMR--QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 460
Cdd:COG4942   92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 461 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERgrqsaeldnrlfkqdfgdKINSLQLEVEALTRQRTQLE 540
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA------------------ELAELQQEAEELEALIARLE 233
                        250       260
                 ....*....|....*....|
gi 576795839 541 LELKQEKERKSQNRGTPGKG 560
Cdd:COG4942  234 AEAAAAAERTPAAGFAALKG 253
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
610-657 6.85e-06

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: 43.82  E-value: 6.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 576795839 610 VCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPSSI---KPERVCNPCH 657
Cdd:cd15760    7 RCDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
382-549 7.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  382 KQDRTAEGQALSEARKHLKEETQLRLDVEKELEL--QISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  460 FKLQSSDLGVKQKSELN---SRLEEKTNQMAATIKQLEQRLRQAERGR---QSAELDNRLFKQDFGDKINSLQlevEALT 533
Cdd:COG4913   696 ELEAELEELEEELDELKgeiGRLEKELEQAEEELDELQDRLEAAEDLArleLRALLEERFAAALGDAVERELR---ENLE 772
                         170
                  ....*....|....*.
gi 576795839  534 RQRTQLELELKQEKER 549
Cdd:COG4913   773 ERIDALRARLNRAEEE 788
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
622-657 7.42e-06

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: 43.96  E-value: 7.42e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSS--IKPERVCNPCH 657
Cdd:cd15733   23 KHHCRNCGNVFCADCSNYKLPIPDEqlYDPVRVCNSCY 60
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-548 8.17e-06

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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.40  E-value: 8.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLDEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   394 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:pfam01576  163 EFTSNLAEEeekakslSKLKNkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   460 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRlfkqDFGDKINSLQLEVE-ALTRQRTQ 538
Cdd:pfam01576  243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALKTELEdTLDTTAAQ 318
                          250
                   ....*....|
gi 576795839   539 LELELKQEKE 548
Cdd:pfam01576  319 QELRSKREQE 328
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-571 9.00e-06

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: 49.30  E-value: 9.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEElavannRIITLQEEMERVKEESSYLLESNRKG 380
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   381 PKQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 447
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   448 LDDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERGRQSAELDnrlfKQD 517
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSK 466
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839   518 FGDKINSLQLEVEALTRQRTQLELELKQ-EKERKSQNRGTPGKGAQKPELRMDGK 571
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEEVLKASIQ 521
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
392-554 1.83e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.02  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  392 LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDV--CEKQDALVSLRQQLDDLRALKHelafklqssdlgv 469
Cdd:COG3096   443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQTARELLRRYRSQQA------------- 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  470 kqkselnsrLEEKTNQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINsLQLEVEALTRQRTQLELELKQEKER 549
Cdd:COG3096   510 ---------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQ 579

                  ....*
gi 576795839  550 KSQNR 554
Cdd:COG3096   580 RSELR 584
PRK11281 PRK11281
mechanosensitive channel MscK;
317-539 2.27e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  317 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEESSY----------LLESNRKGPKQDR- 385
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  386 ------TAEgQALSEA-----RKHLKEETQL------RLDvekELELQISmRQEMELA----------MKMLEKDVCEKQ 438
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRD---YLTARIQ-RLEHQLQllqeainskrLTLSEKTVQEAQ 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  439 DALVSLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERG--------RQSAELD 510
Cdd:PRK11281  267 SQDEAARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLS 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 576795839  511 NRLFKQ-----------DFGDKINSLQLEVEALTRQRTQL 539
Cdd:PRK11281  340 RILYQQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
611-657 3.17e-05

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: 41.72  E-value: 3.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDSLTKNT--CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCH 657
Cdd:cd15749    2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
312-488 3.94e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 312 DQKNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE------SSY-----------LL 374
Cdd:COG3883   31 ELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerarALYrsggsvsyldvLL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 375 ESnrKGPKQ--DR--------TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSL 444
Cdd:COG3883  110 GS--ESFSDflDRlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 576795839 445 RQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAA 488
Cdd:COG3883  188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
622-662 4.05e-05

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: 41.94  E-value: 4.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPCHEQLIK 662
Cdd:cd15739   26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
200-273 4.07e-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 [Multi-domain]  Cd Length: 209  Bit Score: 45.39  E-value: 4.07e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 200 VKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNA-LMMEEEGAIIAGLLVGLNVIDAnFC 273
Cdd:cd17690  130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAfLRCDDEKEQFLYHLLSFNAVDY-FC 203
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
363-552 4.94e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 363 MERVKEESSYLLESNRKGPKQDRTaEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVcEKQDALV 442
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 443 SLRQQLDDLRALKHELAfklqssdlgvkqksELNSRLEEKTNQMAA---TIKQLEQRLRQAERGRQSAELDNRLFKQDFG 519
Cdd:COG4717  126 QLLPLYQELEALEAELA--------------ELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATE 191
                        170       180       190
                 ....*....|....*....|....*....|...
gi 576795839 520 DKINSLQLEVEALTRQRTQLELELKQEKERKSQ 552
Cdd:COG4717  192 EELQDLAEELEELQQRLAELEEELEEAQEELEE 224
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
318-552 7.19e-05

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: 46.17  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  318 EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEG-------- 389
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  390 -------------QALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 448
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  449 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERGRQSAELDNRLFKQDfgdkINSLQLE 528
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
                         250       260
                  ....*....|....*....|....
gi 576795839  529 VEALTRQRTQLELELKQEKERKSQ 552
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRES 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
327-587 8.88e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 406
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 407 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 485
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 486 MAATIKQLEQRLRQAErgrqsaELDNRLFKQDfgDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKgaQKPE 565
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN--EYLE 606
                        250       260
                 ....*....|....*....|..
gi 576795839 566 LRmDGKHRIQEENVKLKKPLEE 587
Cdd:PRK03918 607 LK-DAEKELEREEKELKKLEEE 627
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
610-660 1.05e-04

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: 40.79  E-value: 1.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 576795839 610 VCQLCQEDDSLTKNT---CRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 660
Cdd:cd15755   10 VCMRCQKAKFTPVNRrhhCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
306-612 1.25e-04

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: 45.34  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   306 QITAILDQknyvEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMErvkeessyLLESNRKGPKQDR 385
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE--------LCAAAITCTAQCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   386 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 462
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   463 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQR 536
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839   537 TQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEEnvkLKKPLEESHRLLTHPAEEQGQPSLSEKPQVCQ 612
Cdd:TIGR00618  614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT---LTQERVREHALSIRVLPKELLASRQLALQKMQ 686
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
292-583 2.07e-04

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: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 43.98  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  292 LKDGNSSKGSEGDGQITAILDQknyveelnrhlnatvnnLQTKVDLLEksntkltEELAVANNRIITLQEEMERVKEESS 371
Cdd:pfam09787  30 LKEGSGVEGLDSSTALTLELEE-----------------LRQERDLLR-------EEIQKLRGQIQQLRTELQELEAQQQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  372 YLLESNRkgpkqdrtaegQALSEARKHLKEETQLRLDVEKELElqiSMRQEMElamKMLEKDVCEKQDALVSLRQQLDDL 451
Cdd:pfam09787  86 EEAESSR-----------EQLQELEEQLATERSARREAEAELE---RLQEELR---YLEEELRRSKATLQSRIKDREAEI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  452 RALKHELAFKLQSSdlgvKQKSELNSRLeektnqmaatiKQLEQRLRQAergrqsaeldnrlfkqdfgdkinslQLEVEA 531
Cdd:pfam09787 149 EKLRNQLTSKSQSS----SSQSELENRL-----------HQLTETLIQK-------------------------QTMLEA 188
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 576795839  532 LTRQRTQLELELKQ-EKERKSqnrgTPGKGAQKPELRMDGKHRiqEENVKLKK 583
Cdd:pfam09787 189 LSTEKNSLVLQLERmEQQIKE----LQGEGSNGTSINMEGISD--GEGTRLRN 235
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
334-501 2.16e-04

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: 44.34  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  334 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 394
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 472
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|.
gi 576795839  473 SELNSRLE--EKTNQMAATIKQLEQRLRQAE 501
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEYE 592
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
324-508 2.49e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 324 LNATVN-----NLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAE-GQALSEARK 397
Cdd:COG3206  154 ANALAEayleqNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSElESQLAEARA 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 398 HLKE--------ETQLRLDVEKELELQISM--------RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-LKHELAF 460
Cdd:COG3206  234 ELAEaearlaalRAQLGSGPDALPELLQSPviqqlraqLAELEAELAELSARYTPNHPDVIALRAQIAALRAqLQQEAQR 313
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 576795839 461 KLQSSDLGVK----QKSELNSRLEEkTNQMAATIKQLEQRLRQAERGRQSAE 508
Cdd:COG3206  314 ILASLEAELEalqaREASLQAQLAQ-LEARLAELPELEAELRRLEREVEVAR 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-458 2.73e-04

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: 44.28  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   313 QKNYVEELNRH--LNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNRKGPKQ 383
Cdd:TIGR02168  350 KEELESLEAELeeLEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRRERLQQ 421
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839   384 DRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:TIGR02168  422 EIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
mukB PRK04863
chromosome partition protein MukB;
392-554 3.07e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  392 LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 469
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  470 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAErGRQSAELDNRLFKQDF----GDKINSLQLEVEALTRQRTQLELELK 544
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFC-KRLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|
gi 576795839  545 QEKERKSQNR 554
Cdd:PRK04863  590 QLQARIQRLA 599
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
306-496 3.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  306 QITAILDQKNYVEELNRHLNAtvnnlQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssylLESNRkgpKQDR 385
Cdd:COG4913   266 AARERLAELEYLRAALRLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREE----LDELE---AQIR 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  386 TAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSs 465
Cdd:COG4913   334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA- 412
                         170       180       190
                  ....*....|....*....|....*....|.
gi 576795839  466 dlgvkQKSELNSRLEEKTNQmaatIKQLEQR 496
Cdd:COG4913   413 -----ALRDLRRELRELEAE----IASLERR 434
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
331-500 3.55e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.89  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  331 LQTKVDLLEKSNTKLTE-----ELAVANNRIITLQEEMERVKEESSYLLESNRKGPkqdrTAEGQALSEARKhlKEETQL 405
Cdd:PRK10929  112 LQVSSQLLEKSRQAQQEqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLGTPN----TPLAQAQLTALQ--AESAAL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  406 RLDVEkELEL-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL------QSSDL--GVKQKS 473
Cdd:PRK10929  186 KALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEStellaeQSGDLpkSIVAQF 264
                         170       180
                  ....*....|....*....|....*..
gi 576795839  474 ELNSRLEEKTNQMAATIKQLEQRLRQA 500
Cdd:PRK10929  265 KINRELSQALNQQAQRMDLIASQQRQA 291
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
328-554 4.39e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.59  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  328 VNNLQTKVDLLEKSNTKL-------TEELAVANNRIITLQEEMERVKEE---SSYLLESNRKG---------PKQDRTAE 388
Cdd:pfam07111 164 LSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYvgeqvppevHSQTWELE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  389 GQALSEARKHLKEEtqlRLDVEKELEL-QISMR--------QEMELAMKMLEKDVCEKQDALvSLRQQLDDLRALKHELA 459
Cdd:pfam07111 244 RQELLDTMQHLQED---RADLQATVELlQVRVQslthmlalQEEELTRKIQPSDSLEPEFPK-KCRSLLNRWREKVFALM 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  460 FKLQSSDLgvkqkselnsrleektnQMAATIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKinSLQLEVEALTRQRTQL 539
Cdd:pfam07111 320 VQLKAQDL-----------------EHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDK--AAEVEVERMSAKGLQM 380
                         250
                  ....*....|....*
gi 576795839  540 ELELKQEKERKSQNR 554
Cdd:pfam07111 381 ELSRAQEARRRQQQQ 395
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
400-552 4.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 400 KEETQLRL-----------DVEKELELQI-SMRQEMELAMKML----EKDVCEKQDALVSLRQQLDDLRALKHELAFKLQ 463
Cdd:COG1196  174 KEEAERKLeateenlerleDILGELERQLePLERQAEKAERYRelkeELKELEAELLLLKLRELEAELEELEAELEELEA 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 464 SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL-RQAERGRQSAELDNRlfkqdfgdkINSLQLEVEALTRQRTQLELE 542
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQaEEYELLAELARLEQD---------IARLEERRRELEERLEELEEE 324
                        170
                 ....*....|
gi 576795839 543 LKQEKERKSQ 552
Cdd:COG1196  325 LAELEEELEE 334
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
310-542 6.55e-04

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: 43.13  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   310 ILDQK--NYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYLLESNR--KGPKQDR 385
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   386 TAEGQALSEARKHLKE---ETQLRL-DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFK 461
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEqriDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   462 LQssdlgvKQKSELNsRLEEKTNQMAATIKQLEQRLRQAErgrqsaeldnRLFKQDFGDKINSLQLEVEALTRQRTQLEL 541
Cdd:TIGR02169  905 IE------ELEAQIE-KKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967

                   .
gi 576795839   542 E 542
Cdd:TIGR02169  968 R 968
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
421-549 7.12e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 421 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 500
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREELGERARAL 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 501 ERGRQSAELDNRLFK-QDFGDKINSLQLeVEALTRQRTQLELELKQEKER 549
Cdd:COG3883   96 YRSGGSVSYLDVLLGsESFSDFLDRLSA-LSKIADADADLLEELKADKAE 144
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
611-656 7.89e-04

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: 37.92  E-value: 7.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 576795839 611 CQLCQEDDS--LTKNTCRNCRGTFCNACTTNELPLPSSIKPERVCNPC 656
Cdd:cd15726   10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
611-656 8.28e-04

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: 37.87  E-value: 8.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 611 CQLCQEDDSLT--KNTCRNCRGTFCNACTTNELPLPSSIKP--ERVCNPC 656
Cdd:cd15745    2 CAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLSVPDTCiyLRVCKTC 51
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
318-555 8.58e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 8.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   318 EELNRHLNATVNNLQT----KVDLLEKSNTKLtEELavannRIITLQEEmERVKEESSYLLE----SNRKGPKQDRTAE- 388
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE-GVLQEIRSILVDfeeaSGKKIYEHDSMSTm 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   389 -----GQALSEARKHLKEETQLR----LDVEKELE-LQISMRQEMELAMKM----LEKDVCEKQDALVSLRQQLDDLRAL 454
Cdd:pfam15921  214 hfrslGSAISKILRELDTEISYLkgriFPVEDQLEaLKSESQNKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARSQ 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   455 KHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSA--ELDNRL----------------FKQ 516
Cdd:pfam15921  294 ANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFSQ 370
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 576795839   517 DFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRG 555
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG 409
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
310-552 1.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 310 ILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIitlqEEMERVKEESSYLLESNRKGPKQDRTAEg 389
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLE- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 390 QALSEARKHLkEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 469
Cdd:PRK03918 259 EKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 470 KQKSELNSRLEEKTNQMAAtikqLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKER 549
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                 ...
gi 576795839 550 KSQ 552
Cdd:PRK03918 414 IGE 416
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
341-606 1.19e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.13  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   341 SNTKLTEELAVANNriiTLQEEMERVKEESSYLLESNRKGPKQDRtaegqALSEARKHLK--EETQLRLDVEKELElqis 418
Cdd:pfam12128  598 SEEELRERLDKAEE---ALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKnaRLDLRRLFDEKQSE---- 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   419 mrqemelaMKMLEKDVCEKQDALVSLRQQLD-DLRALKHEL-----AFKLQSSDLGVKQKSELNSRLEEKTNQMAAT--- 489
Cdd:pfam12128  666 --------KDKKNKALAERKDSANERLNSLEaQLKQLDKKHqawleEQKEQKREARTEKQAYWQVVEGALDAQLALLkaa 737
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   490 ---------------------------------------IKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVE 530
Cdd:pfam12128  738 iaarrsgakaelkaletwykrdlaslgvdpdviaklkreIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS 817
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839   531 ALTRQRTQLELELK---QEKERKSQNRGTPGKGAQKPELRMDGKHRiqeenvKLKKPLEESHRLLTHPAEEQGQPSLSE 606
Cdd:pfam12128  818 NIERAISELQQQLArliADTKLRRAKLEMERKASEKQQVRLSENLR------GLRCEMSKLATLKEDANSEQAQGSIGE 890
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
339-551 1.63e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 339 EKSNTKLTEELAVANNriiTLQEEMERVKEESSYLLESNRKGPKQDR-TAEGQALSEARKHLKEETQLRLDVEKELELQI 417
Cdd:COG5185  335 ETGIQNLTAEIEQGQE---SLTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQNQRGYAQEILATL 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 418 smrqemELAMKMLEKDVCEKQDALVSLRQQLDD----LRALKHELAFKLQSSDLGVKQK-----SELNSRLEEKTNQMAA 488
Cdd:COG5185  412 ------EDTLKAADRQIEELQRQIEQATSSNEEvsklLNELISELNKVMREADEESQSRleeayDEINRSVRSKKEDLNE 485
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576795839 489 TIKQLEQRLRQAERGRQSAELDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKS 551
Cdd:COG5185  486 ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
605-660 1.75e-03

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


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 37.33  E-value: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576795839 605 SEKPQvCQLCQEDDSLTK--NTCRNCRGTFCNACTTNELPLPS-SIKPERVCNPCHEQL 660
Cdd:cd15729   11 SEAPN-CMQCEVKFTFTKrrHHCRACGKVLCSACCSLKARLEYlDNKEARVCVPCYQTL 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
338-513 1.86e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 338 LEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLlESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQI 417
Cdd:COG4372   15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 418 SMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL 497
Cdd:COG4372   94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
                        170
                 ....*....|....*.
gi 576795839 498 RQAERGRQSAELDNRL 513
Cdd:COG4372  174 QALSEAEAEQALDELL 189
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
622-657 2.09e-03

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: 36.92  E-value: 2.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 576795839 622 KNTCRNCRGTFCNACTTNELPLPS--SIKPERVCNPCH 657
Cdd:cd15738   24 KHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
317-496 2.33e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 317 VEELNRHLNATVNNLqtkVDLLE----------KSNTKLTEELAVANNRIITLQEEMERVKEesSYLL-----ESNRKGP 381
Cdd:PRK04778 280 AEEKNEEIQERIDQL---YDILErevkarkyveKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 382 KQ------------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElelQISMRQEmelaMKMLEKDvcEKQdalvsLRQQ 447
Cdd:PRK04778 355 KQleslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREK 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 576795839 448 LDDLRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 496
Cdd:PRK04778 420 LERYRNKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
318-547 2.44e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.28  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 318 EELNRHLNATVNNLQTKVDLLEKSNTKLTE---ELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqdrtaEGQALSE 394
Cdd:COG1340   46 DELNAQVKELREEAQELREKRDELNEKVKElkeERDELNEKLNELREELDELRKELAELNKAGG---------SIDKLRK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 395 ARKHLKEETQ---LRLDVEKELELQIS-MRQEMELAMKMLE--KDVCEKQDALVSLRQQLDDLRALKHELAFKLQS-SDL 467
Cdd:COG1340  117 EIERLEWRQQtevLSPEEEKELVEKIKeLEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQElHEE 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 468 GVKQKSELNSrLEEKTNQMAATIKQLeqrlrQAERGRQSAELDNRLFK-QDFGDKINSLQLEVEALTRQRTQLELELKQE 546
Cdd:COG1340  197 MIELYKEADE-LRKEADELHKEIVEA-----QEKADELHEEIIELQKElRELRKELKKLRKKQRALKREKEKEELEEKAE 270

                 .
gi 576795839 547 K 547
Cdd:COG1340  271 E 271
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
322-606 2.52e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  322 RHLNATVNNLQTKVDLLEKSNTKLTEELavaNNRIITLQEEMERVKEessylLESNRKGPKQDRTAEGQALSEARK---H 398
Cdd:pfam10174 383 RDLKDMLDVKERKINVLQKKIENLQEQL---RDKDKQLAGLKERVKS-----LQTDSSNTDTALTTLEEALSEKERiieR 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  399 LKEETQlRLDVEKELELQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELN 476
Cdd:pfam10174 455 LKEQRE-REDRERLEELESLKKENKDLKEKVsaLQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEC 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  477 SRLE---EKTNQMAAT----------IKQLEQ--RLRQAERGRQSAELDnRLfkqdfgdkINSL-QLEVEALTRQRTQLE 540
Cdd:pfam10174 534 SKLEnqlKKAHNAEEAvrtnpeindrIRLLEQevARYKEESGKAQAEVE-RL--------LGILrEVENEKNDKDKKIAE 604
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795839  541 LELKQEKERKSQNRgtpgKGAQKpelrmdgKHRIQEENVKLKKPLEESHRLLTHPAEEQGQPSLSE 606
Cdd:pfam10174 605 LESLTLRQMKEQNK----KVANI-------KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEE 659
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
328-556 2.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 328 VNNLQTKVDLLEKSNTKLTE----ELAVANNRIITLQEEMERVKEESSYLLESNRKgpkqdrtaegqaLSEARKHLKEET 403
Cdd:COG4717   48 LERLEKEADELFKPQGRKPElnlkELKELEEELKEAEEKEEEYAELQEELEELEEE------------LEELEAELEELR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 404 QLRLDVEKELELQISMRQEMELAMKMLEKDVC--EKQDALVSLRQQLDDLRALKHELAfklqssdlgvKQKSELNSRLEE 481
Cdd:COG4717  116 EELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELA----------ELQEELEELLEQ 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576795839 482 KTNQMAATIKQLEQRLRQAERGRQSAEldnrlfkqdfgDKINSLQLEVEALTRQRTQLE--LELKQEKERKSQNRGT 556
Cdd:COG4717  186 LSLATEEELQDLAEELEELQQRLAELE-----------EELEEAQEELEELEEELEQLEneLEAAALEERLKEARLL 251
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
322-547 3.19e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  322 RHLNATVNNLQTKVDLLEKSNTKLTeelavANNRIITLqEEMERVKEESSYLLE--SNRKGPKQDRTAEGQALSEARKHL 399
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELT-----AHCDKLLL-ENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLE 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  400 KEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRL 479
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576795839  480 EEKTNQMAATIKQLEQRLRQAERGRQSAeldnrlfKQDFGDKINSLQLEVEALTRQRTQLELELKQEK 547
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASA-------KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
343-554 4.65e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   343 TKLTEELAVANNRIITLQEEMERVKEessYLLESNRKGPKQDRTAEgqaLSEARKHLKEE-TQLRLDVE-KELELQISMR 420
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED---ILNELERQLKSLERQAE---KAERYKELKAElRELELALLvLRLEELREEL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839   421 QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQS--SDLG--VKQKSELNSRLEEKTNQMAATIKQLEQR 496
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYalANEISRLEQQKQILRERLANLERQLEEL 321
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 576795839   497 LRQAERGRQSAELDNRLFKQdFGDKINSLQLEVEALtrqRTQLELELKQEKERKSQNR 554
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAE-LEEKLEELKEELESL---EAELEELEAELEELESRLE 375
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-599 4.77e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 317 VEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALSEAR 396
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ-EELESLQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 397 KHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKsELN 476
Cdd:COG4372  108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ-ALD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 477 SRLEEKTNQMAATIKQLEQRLRQAERGRQSAEldnRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGT 556
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELAE---ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 576795839 557 PGKGAQKPELRMDGKHRIQEENVKLKKPLEESHRLLTHPAEEQ 599
Cdd:COG4372  264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
360-607 4.82e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  360 QEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEEtqlRLDVEKELELQiSMRQE-----------MELAMK 428
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE---RMAMERERELE-RIRQEerkrelerirqEEIAME 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  429 M-----LEKDVCEKQDALVSLRQQLDDLRALK---HELAFKLQssdlgvKQKSELNSRLEEKTNQMAATIKQLEQ-RLRQ 499
Cdd:pfam17380 374 IsrmreLERLQMERQQKNERVRQELEAARKVKileEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEeRARE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  500 AERGRQsaeldnrlfkqdfgdkinslqlevEALTRQRtQLELELKQEKERKSQnrgtpgKGAQKPELRmdGKHRIQEENV 579
Cdd:pfam17380 448 MERVRL------------------------EEQERQQ-QVERLRQQEEERKRK------KLELEKEKR--DRKRAEEQRR 494
                         250       260
                  ....*....|....*....|....*....
gi 576795839  580 K-LKKPLEESHRLLThpaEEQGQPSLSEK 607
Cdd:pfam17380 495 KiLEKELEERKQAMI---EEERKRKLLEK 520
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
323-372 6.96e-03

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.


Pssm-ID: 463001  Cd Length: 523  Bit Score: 39.42  E-value: 6.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 576795839  323 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKeeSSY 372
Cdd:pfam10212 443 HFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQDELTTTK--RSY 490
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
227-551 7.01e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  227 SEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQvgvidfsmyLKDGNSSKGSEgDGQ 306
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---------MEELNKAKAAH-SFV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  307 ITAILDQKNYVEELNRHLNATVNNLQTKVDL----LEKSNTKLTEELAVANNRIITLqEEMERVKEESSYLLESNR---- 378
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIitmeLQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKqfek 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  379 -----KGPKQDRTAEGQA---------------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQ 438
Cdd:pfam05483 430 iaeelKGKEQELIFLLQArekeihdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  439 DALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERGRQSAE---LDNRLFK 515
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEyevLKKEKQM 589
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 576795839  516 QDFGDKINSLQLEVEALTRQRTQLELELKQEKERKS 551
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
324-552 7.32e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.78  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  324 LNATVNnlQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESnrkgpKQDRTAEGQALSEA---RKHLK 400
Cdd:PRK10246  523 LEPGVN--QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE-----EQALTQQWQAVCASlniTLQPQ 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  401 EETQLRLDVEKELELQ---ISMRQEMELAMKMLEKDVCEKQDALVSLRQQL-DDLRALKHE----------LAFKLQSSD 466
Cdd:PRK10246  596 DDIQPWLDAQEEHERQlrlLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLlTALAGYALTlpqedeeaswLATRQQEAQ 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  467 LGVKQKSELNsRLEEKTNQMAATIKQLEQRlRQAERGRQSAELDNRlfkQDFGDKINSLQLEVEALTRQRTqlelelkQE 546
Cdd:PRK10246  676 SWQQRQNELT-ALQNRIQQLTPLLETLPQS-DDLPHSEETVALDNW---RQVHEQCLSLHSQLQTLQQQDV-------LE 743

                  ....*.
gi 576795839  547 KERKSQ 552
Cdd:PRK10246  744 AQRLQK 749
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
331-516 7.37e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 331 LQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssylLESNRkgpKQDRTAEGQaLSEARKHLK--EETQLRLD 408
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLE---KEIKRLELE-IEEVEARIKkyEEQLGNVR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 409 VEKELElqiSMRQEMELA---MKMLEKDVCEKQDALVSLRQQLDDLRAlkhelafklqssdlgvkQKSELNSRLEEKTNQ 485
Cdd:COG1579   87 NNKEYE---ALQKEIESLkrrISDLEDEILELMERIEELEEELAELEA-----------------ELAELEAELEEKKAE 146
                        170       180       190
                 ....*....|....*....|....*....|...
gi 576795839 486 MAATIKQLEQRL--RQAERGRQSAELDNRLFKQ 516
Cdd:COG1579  147 LDEELAELEAELeeLEAEREELAAKIPPELLAL 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
318-509 8.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 318 EELNRHLNATVNNLQTKVDLLEKSntklTEELAVANNRIITLQEEMERVKEESSYLL-ESNRKGPKQDRTAEGQaLSEAR 396
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEER-LKELE 598
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839 397 KHLKEETQLRlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlQSSDLGVKQKSELN 476
Cdd:PRK03918 599 PFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLELSRELA 676
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 576795839 477 S------RLEEKTNQMAATIKQLEQRLRQAERGRQSAEL 509
Cdd:PRK03918 677 GlraeleELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
327-552 9.60e-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: 39.23  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESsyllesnrKGPKQDRTAEGQALSEARKHLKEETQLR 406
Cdd:TIGR04523  69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI--------KNDKEQKNKLEVELNKLEKQKKENKKNI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  407 LDV-------EKELELQ-------ISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDL--------------RALKHEL 458
Cdd:TIGR04523 141 DKFlteikkkEKELEKLnnkyndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkkiqknKSLESQI 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795839  459 A-FKLQSSDLGvKQKSELNSRLEEKTNQMAATIKQLEQRL-------RQAERGRQSAELDNRLFKQdFGDKINSLQLEVE 530
Cdd:TIGR04523 221 SeLKKQNNQLK-DNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikKQLSEKQKELEQNNKKIKE-LEKQLNQLKSEIS 298
                         250       260
                  ....*....|....*....|....*..
gi 576795839  531 ALTRQRTQ-----LELELKQEKERKSQ 552
Cdd:TIGR04523 299 DLNNQKEQdwnkeLKSELKNQEKKLEE 325
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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