NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568972939|ref|XP_006532904|]
View 

RUN and FYVE domain-containing protein 1 isoform X1 [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_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
23-178 1.40e-103

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: 310.30  E-value: 1.40e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17694   81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
545-615 3.11e-48

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: 162.54  E-value: 3.11e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 545 LKGHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 615
Cdd:cd15758    1 LKGHAWLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
237-540 6.13e-14

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.48  E-value: 6.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   237 QTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEksveitkqdtkveletykQTRQGLDEMYSDVWK 316
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------------------ELSRQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   317 QLKEEKKVRLELEKELELQigmkTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIA 396
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   397 SFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQ---ELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQ 473
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939   474 RELQrekdtscLLQTELQQVEglkKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKE 540
Cdd:TIGR02168  887 EALA-------LLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
 
Name Accession Description Interval E-value
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
23-178 1.40e-103

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: 310.30  E-value: 1.40e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17694   81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
545-615 3.11e-48

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: 162.54  E-value: 3.11e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 545 LKGHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 615
Cdd:cd15758    1 LKGHAWLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
58-181 9.19e-41

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: 144.73  E-value: 9.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   58 QFFVVMEHCLKHGLKV------KKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTA---VGRGRAWLYLALMQ 128
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTPyspDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568972939  129 KKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGLNVLDANLCLKG 181
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
550-612 3.90e-26

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: 101.69  E-value: 3.90e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939  550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALP---SYPKPVRVCDSCHTLLLQ 612
Cdd:pfam01363   3 WVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQK 68
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
548-610 3.36e-25

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: 99.04  E-value: 3.36e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568972939   548 HTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPS--YPKPVRVCDSCHTLL 610
Cdd:smart00064   2 PHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKlgIERPVRVCDDCYENL 66
RUN smart00593
domain involved in Ras-like GTPase signaling;
118-180 3.10e-15

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 70.34  E-value: 3.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939   118 GRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGLNVLDANLCLK 180
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGeQLLGLLVGLSALDFNLPVD 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
237-540 6.13e-14

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: 75.48  E-value: 6.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   237 QTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEksveitkqdtkveletykQTRQGLDEMYSDVWK 316
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------------------ELSRQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   317 QLKEEKKVRLELEKELELQigmkTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIA 396
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   397 SFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQ---ELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQ 473
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939   474 RELQrekdtscLLQTELQQVEglkKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKE 540
Cdd:TIGR02168  887 EALA-------LLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
349-512 2.56e-12

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 69.66  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 349 LEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQ--QKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAA 426
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRK-------ELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 427 EERSHKLQQELSGRGSALQL-----QLSQLRDQCSGLEKELKSE--------------KEQRQALQRELQREKDTscLLQ 487
Cdd:COG3206  239 EARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELsarytpnhpdvialRAQIAALRAQLQQEAQR--ILA 316
                        170       180
                 ....*....|....*....|....*
gi 568972939 488 TELQQVEGLKKELRELQDEKAELRK 512
Cdd:COG3206  317 SLEAELEALQAREASLQAQLAQLEA 341
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
233-545 4.10e-11

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: 66.35  E-value: 4.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   233 VGDLQTKIDGLEKTNSKLQEELSAATDRicsLQKEQQQLREQNEVIRErseksVEITKQDTKVELETYKQTRQGLDEMYS 312
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRE-----LEAQISELQEDLESERAARNKAEKQRR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   313 DVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLL------EKDTHEKQ---------DTLVALRQQLEEVKAINLQM 377
Cdd:pfam01576  296 DLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELkkaleeETRSHEAQlqemrqkhtQALEELTEQLEQAKRNKANL 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   378 FHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQ-------QAERARQAAEERSHKLQQELSGRGSALqlqlSQ 450
Cdd:pfam01576  376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQelqarlsESERQRAELAEKLSKLQSELESVSSLL----NE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   451 LRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQemgLHLSQ 530
Cdd:pfam01576  452 AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ---AQLSD 528
                          330
                   ....*....|....*
gi 568972939   531 SKLKMEDIKEVNKAL 545
Cdd:pfam01576  529 MKKKLEEDAGTLEAL 543
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
199-524 8.21e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 8.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 199 DAQDLDSGREHERiTDVLDQKNYVEELN---RHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEqqqLREQN 275
Cdd:PRK02224 364 EAAELESELEEAR-EAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT---LRTAR 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 276 EVIRErSEKSVEITK-----QDTK----VE-LETYKQTRQGLDEMYSDVWKQLKE-EKKV-RLELEKELELQIG-MKTEM 342
Cdd:PRK02224 440 ERVEE-AEALLEAGKcpecgQPVEgsphVEtIEEDRERVEELEAELEDLEEEVEEvEERLeRAEDLVEAEDRIErLEERR 518
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 343 EIAMKLL---EKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQME---ERL 416
Cdd:PRK02224 519 EDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirTLL 598
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 417 QQAERARQAAEERSHKLQQeLSGRGSALQLQLSQLRDQCSGLE--------KELKSEKEQRQALQ-------RELQREKD 481
Cdd:PRK02224 599 AAIADAEDEIERLREKREA-LAELNDERRERLAEKRERKRELEaefdeariEEAREDKERAEEYLeqveeklDELREERD 677
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568972939 482 TsclLQTELQQVEGLKKELRELQDEKAELRKVCE------EQEQALQEM 524
Cdd:PRK02224 678 D---LQAEIGAVENELEELEELRERREALENRVEalealyDEAEELESM 723
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
541-607 3.89e-05

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 47.00  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  541 VNKALKGHTWLKDDEAT-HCKQCEKDF-SISR----RKHHCRNCGHIFCNTC-------SSNELALPSYPKPVR---VCD 604
Cdd:PTZ00303  444 LTKLLHNPSWQKDDESSdSCPSCGRAFiSLSRplgtRAHHCRSCGIRLCVFCitkrahySFAKLAKPGSSDEAEerlVCD 523

                  ...
gi 568972939  605 SCH 607
Cdd:PTZ00303  524 TCY 526
 
Name Accession Description Interval E-value
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
23-178 1.40e-103

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: 310.30  E-value: 1.40e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17694    1 ERANLMNMMKLSIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17694   81 TSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
23-178 1.30e-88

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: 271.85  E-value: 1.30e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17695    1 ERANLLNMAKLSIKGLIESALSFGRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17695   81 ASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEEGAVIVGLLVGLNVIDANLC 156
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
23-177 3.57e-87

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: 267.90  E-value: 3.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17681    1 ERRNLLNLAKLSIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANL 177
Cdd:cd17681   81 ASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVVIAGLLVGLNVIDCNL 155
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
23-178 2.87e-79

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: 247.60  E-value: 2.87e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  23 ERANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA 102
Cdd:cd17696    1 ERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17696   81 ASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEEGAIIAGLLVGLNVIDANFC 156
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
545-615 3.11e-48

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: 162.54  E-value: 3.11e-48
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 545 LKGHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 615
Cdd:cd15758    1 LKGHAWLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
58-181 9.19e-41

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: 144.73  E-value: 9.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   58 QFFVVMEHCLKHGLKV------KKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTA---VGRGRAWLYLALMQ 128
Cdd:pfam02759   1 QLCAALEALLSHGLKRssllilRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTPyspDGRGRAWIRLALNE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568972939  129 KKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGLNVLDANLCLKG 181
Cdd:pfam02759  81 KLLDQWLKLLLSNKELLSEYYEPWALLADPEFGeILLGLLVGLSALDFNLCLKL 134
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
550-607 8.61e-37

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: 130.97  E-value: 8.61e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCH 607
Cdd:cd15721    1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
547-616 1.17e-33

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: 122.83  E-value: 1.17e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 547 GHTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSS 616
Cdd:cd15759    1 GQVWLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSS 70
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
34-177 2.78e-28

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: 110.59  E-value: 2.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  34 SIKVLLQSALSLGR-------SLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQnKSFFGPLELVEKLCPEASDIAT--S 104
Cdd:cd17671    2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKPKRFGGGK-VSFWDFLEALEKLLPAPSLKQAirD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939 105 VRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMV-IVGLLVGLNVLDANL 177
Cdd:cd17671   81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAElFLSLLVGLSSLDFNL 154
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
548-610 7.24e-28

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: 106.33  E-value: 7.24e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 548 HTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLL 610
Cdd:cd15730    1 RKWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
26-177 3.28e-26

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: 104.79  E-value: 3.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  26 NLMHMMKLSIKVLLQSALSlgRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIG--QNKSFFGPLELVEKLCPEASdIAt 103
Cdd:cd17684    1 NLVTVCRLSVKSLIDKACL--ETIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC-IA- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939 104 SVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANL 177
Cdd:cd17684   77 SIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSEDATVLCGMLIGLNAIDFSF 150
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
550-612 3.90e-26

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: 101.69  E-value: 3.90e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939  550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALP---SYPKPVRVCDSCHTLLLQ 612
Cdd:pfam01363   3 WVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQK 68
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
548-610 3.36e-25

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: 99.04  E-value: 3.36e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568972939   548 HTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPS--YPKPVRVCDSCHTLL 610
Cdd:smart00064   2 PHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKlgIERPVRVCDDCYENL 66
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
550-606 3.39e-23

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: 93.18  E-value: 3.39e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSY--PKPVRVCDSC 606
Cdd:cd15731    5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYgqMKPVRVCNHC 63
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
550-606 7.60e-22

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: 88.93  E-value: 7.60e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPS--YPKPVRVCDSC 606
Cdd:cd15734    2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSrgWDHPVRVCDPC 60
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
550-607 1.11e-21

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: 88.64  E-value: 1.11e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALP--SYPKPVRVCDSCH 607
Cdd:cd15733    1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPdeQLYDPVRVCNSCY 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
550-610 3.38e-21

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: 87.44  E-value: 3.38e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCHTLL 610
Cdd:cd15719    3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRisRPVRVCQACYNIL 65
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
555-607 2.88e-20

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: 84.66  E-value: 2.88e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 555 EATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALP---SYPKPVRVCDSCH 607
Cdd:cd15760    4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPhlgPLGVPQRVCDRCF 59
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
550-610 1.62e-19

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: 82.77  E-value: 1.62e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNelALPSYP--KPVRVCDSCHTLL 610
Cdd:cd15739    4 WQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTK--TVPSGPnrRPARVCDVCHTLL 64
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
549-607 2.03e-19

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: 82.03  E-value: 2.03e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 549 TWLKDDEATHCKQCEK-DFSISRRKHHCRNCGHIFCNTCSSNELALPS-YPKPVRVCDSCH 607
Cdd:cd15717    1 VWVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
26-178 4.80e-19

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: 84.31  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  26 NLMHMMKLSIKVLLQSALSlgRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFI---GQnKSFFGPLELVEKLCPeaSDIA 102
Cdd:cd17699    1 NLITVCRFSVKTLLEKYTA--EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFssdGQ-RGFWDYIRLACSKVP--NNCI 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17699   76 SSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREESTVLTGMLIGLSAIDFSFC 151
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
558-607 1.26e-18

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: 79.50  E-value: 1.26e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568972939 558 HCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPS--YPKPVRVCDSCH 607
Cdd:cd00065    1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
549-606 3.98e-18

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: 78.57  E-value: 3.98e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 549 TWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALP--SYPKPVRVCDSC 606
Cdd:cd15727    3 PWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
26-178 4.79e-18

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: 81.17  E-value: 4.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  26 NLMHMMKLSIKVLLQSalSLGRSLDADYAPLQQFFVVMEHCLKHGLKVKKSFIGQN--KSFFgplELVEKLCPEAS-DIA 102
Cdd:cd17700    1 NLITVCRFSVKTLIDR--SCFETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGYEspRSFW---DYIRVACSKVPhNCI 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 103 TSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLC 178
Cdd:cd17700   76 CSIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFC 151
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
549-607 8.88e-18

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: 77.43  E-value: 8.88e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 549 TWLKDDEathCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSY--PKPVRVCDSCH 607
Cdd:cd15720    1 EWKDGDE---CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCY 58
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
550-606 1.05e-17

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: 77.25  E-value: 1.05e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSC 606
Cdd:cd15732    2 WVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSC 60
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
550-610 3.98e-17

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: 75.84  E-value: 3.98e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 550 WLKDDEATHCKQCEK-DFSISRRKHHCRNCGHIFCNTCSSNELALPSY-PKPVRVCDSCHTLL 610
Cdd:cd15755    2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSQsSKPVRVCDFCYDLL 64
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
559-607 1.06e-16

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: 74.49  E-value: 1.06e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 559 CKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCH 607
Cdd:cd15735    9 CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGinQPVRVCDGCY 59
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
549-613 5.88e-16

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


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 72.38  E-value: 5.88e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568972939 549 TWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSnelalpSYPKPVRVCDSCHTLLLQR 613
Cdd:cd15716    3 PWVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQ------FLPLHIRCCHHCKDLLERR 61
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
550-607 7.73e-16

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


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 71.97  E-value: 7.73e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNEL--ALPSYPKPVRVCDSCH 607
Cdd:cd15725    2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIpgKFIGYPGDLRVCTYCC 61
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
550-606 1.00e-15

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: 71.44  E-value: 1.00e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 606
Cdd:cd15726    1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
549-610 2.60e-15

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: 70.85  E-value: 2.60e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 549 TWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP-KPVRVCDSCHTLL 610
Cdd:cd15729    6 VWVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSLKARLEYLDnKEARVCVPCYQTL 68
RUN smart00593
domain involved in Ras-like GTPase signaling;
118-180 3.10e-15

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 70.34  E-value: 3.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939   118 GRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGLNVLDANLCLK 180
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGeQLLGLLVGLSALDFNLPVD 64
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
555-610 7.93e-15

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


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 69.37  E-value: 7.93e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939 555 EATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSY--PKPVRVCDSCHTLL 610
Cdd:cd15728    6 DGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFdlNKPVRVCDVCFDVL 63
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
549-610 4.82e-14

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


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 67.13  E-value: 4.82e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939 549 TWLKDDEATHCKQCEKDF-SISRRKHHCRNCGHIFCNTCSSNELALP-SYPKPVRVCDSCHTLL 610
Cdd:cd15741    2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKATLEyDGNKLNRVCKHCYVIL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
237-540 6.13e-14

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: 75.48  E-value: 6.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   237 QTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEksveitkqdtkveletykQTRQGLDEMYSDVWK 316
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------------------ELSRQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   317 QLKEEKKVRLELEKELELQigmkTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIA 396
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALD 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   397 SFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQ---ELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQ 473
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939   474 RELQrekdtscLLQTELQQVEglkKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKE 540
Cdd:TIGR02168  887 EALA-------LLRSELEELS---EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
550-606 1.28e-13

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


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 65.54  E-value: 1.28e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP-KPVRVCDSC 606
Cdd:cd15743    3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLKnKSARVCDEC 60
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
559-607 2.63e-13

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: 64.36  E-value: 2.63e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 559 CKQCEKD-FSISRRKHHCRNCGHIFCNTCSSNELALPSY-PKPVRVCDSCH 607
Cdd:cd15744    2 CSLCQEDfASLALPKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
548-607 6.50e-13

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: 63.50  E-value: 6.50e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972939 548 HTWLKDDEATHCkQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCH 607
Cdd:cd15738    1 LDWKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLsqRPVPVCRACY 61
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
50-171 1.02e-12

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: 66.10  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  50 DADYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLE-LVEKLCPEA---SDIATSVRNLPELKTAVGRGRAWLYLA 125
Cdd:cd17682   18 DPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEeLLKKLNKIPkslSDAVKFVKSCKKVKTNQGRGRLFIRYA 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568972939 126 LMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEE-GMVIVGLLVGLN 171
Cdd:cd17682   98 LNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEIlSEILLSLLYQLN 144
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
550-607 1.53e-12

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


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 62.53  E-value: 1.53e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 550 WLKDDEATHCKQCEKD-FSISRRKHHCRNCGHIFCNTCSSNELALPSY-PKPVRVCDSCH 607
Cdd:cd15724    1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYrENPVRVCDQCY 60
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
349-512 2.56e-12

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 69.66  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 349 LEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQ--QKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAA 426
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRK-------ELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 427 EERSHKLQQELSGRGSALQL-----QLSQLRDQCSGLEKELKSE--------------KEQRQALQRELQREKDTscLLQ 487
Cdd:COG3206  239 EARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELsarytpnhpdvialRAQIAALRAQLQQEAQR--ILA 316
                        170       180
                 ....*....|....*....|....*
gi 568972939 488 TELQQVEGLKKELRELQDEKAELRK 512
Cdd:COG3206  317 SLEAELEALQAREASLQAQLAQLEA 341
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
550-610 3.97e-12

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 61.51  E-value: 3.97e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 550 WLKDDEATHCKQC-EKDFSISRRKHHCRNCGHIFCNTCSSNELALPSY-PKPVRVCDSCHTLL 610
Cdd:cd15754    2 WIPDKATDICMRCtQTNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRLsPKPVRVCSLCYRKL 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
207-518 1.03e-11

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: 68.16  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   207 REHERITDVLDQKNYVEELNRHLSctVGDLQTKIDGLEKtnskLQEELSAATDRICSLQKEQQQLREQ-NEVIRERSEKS 285
Cdd:TIGR02168  207 RQAEKAERYKELKAELRELELALL--VLRLEELREELEE----LQEELKEAEEELEELTAELQELEEKlEELRLEVSELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   286 VEITKQDTkvELETYKQTRQGLD---EMYSDVWKQLKEEKKVRLELEKELELQigmKTEMEIAMKLLEKDTHEKQDTLVA 362
Cdd:TIGR02168  281 EEIEELQK--ELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELESK---LDELAEELAELEEKLEELKEELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   363 LRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQaaeershKLQQELSGRGS 442
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE-------RLQQEIEELLK 428
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939   443 ALQ-LQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQvegLKKELRELQDEKAELRKVCEEQE 518
Cdd:TIGR02168  429 KLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARLDSLERLQENLE 502
RUN_FYCO1 cd17698
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
52-171 1.43e-11

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: 62.79  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  52 DYAPLQQFFVVMEHCLKHGLKVKKSFIGQNKS----FFGPLELVEKLcpeaSDIATSVRNLPELKTAVGRGRAWLYLALM 127
Cdd:cd17698   32 DSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDywdyFCECLAKVKGL----NDGIRFVKSLKEVRTSLGKGRAFIRYSLV 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568972939 128 QKKLADYLKVLIDNKQLLSEFYEPE-ALMMEEEGMVIVGLLVGLN 171
Cdd:cd17698  108 HQRLADTLQQCVMNGKVTSDWYYPRsVFLNHKYSSDIINSLYDLN 152
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
209-524 3.78e-11

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: 66.23  E-value: 3.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   209 HERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSvei 288
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--- 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   289 tkQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEmeiAMKLLEKDTHEKQDTLVALRQQL- 367
Cdd:TIGR02168  774 --EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE---RLESLERRIAATERRLEDLEEQIe 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   368 ---EEVKAINLQMFH----------KVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQ 434
Cdd:TIGR02168  849 elsEDIESLAAEIEEleelieelesELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   435 QELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDtscLLQTELQQV-----------EGLKKELREL 503
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK---RLENKIKELgpvnlaaieeyEELKERYDFL 1005
                          330       340
                   ....*....|....*....|.
gi 568972939   504 QDEKAELRKVCEEQEQALQEM 524
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
235-556 3.98e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 235 DLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEiTKQDTKVELETYKQTRQGLDEMYSDV 314
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 315 WKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEA 394
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-------ELAEAEEELEELAEE 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 395 IASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELsgrgsalqLQLSQLRDQcsglekELKSEKEQRQALQR 474
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL--------AELEEEEEE------EEEALEEAAEEEAE 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 475 ELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDD 554
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533

                 ..
gi 568972939 555 EA 556
Cdd:COG1196  534 AA 535
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
233-545 4.10e-11

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: 66.35  E-value: 4.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   233 VGDLQTKIDGLEKTNSKLQEELSAATDRicsLQKEQQQLREQNEVIRErseksVEITKQDTKVELETYKQTRQGLDEMYS 312
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRE-----LEAQISELQEDLESERAARNKAEKQRR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   313 DVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLL------EKDTHEKQ---------DTLVALRQQLEEVKAINLQM 377
Cdd:pfam01576  296 DLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELkkaleeETRSHEAQlqemrqkhtQALEELTEQLEQAKRNKANL 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   378 FHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQ-------QAERARQAAEERSHKLQQELSGRGSALqlqlSQ 450
Cdd:pfam01576  376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQelqarlsESERQRAELAEKLSKLQSELESVSSLL----NE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   451 LRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQemgLHLSQ 530
Cdd:pfam01576  452 AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ---AQLSD 528
                          330
                   ....*....|....*
gi 568972939   531 SKLKMEDIKEVNKAL 545
Cdd:pfam01576  529 MKKKLEEDAGTLEAL 543
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
24-177 4.25e-11

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: 61.84  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  24 RANLMHMMKLSIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKvkKSFIGQNKSFFGPLelVEKLcPEAS---- 99
Cdd:cd17679    1 KKSLTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLK--DKFISKVSSVFSGD--VDKL-PEPNfwpl 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 100 -------DIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGLN 171
Cdd:cd17679   76 llkfshrDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLdILKSLLQGLE 155

                 ....*.
gi 568972939 172 VLDANL 177
Cdd:cd17679  156 SFQFEL 161
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
63-171 7.81e-11

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


Pssm-ID: 439059  Cd Length: 150  Bit Score: 60.58  E-value: 7.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  63 MEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNK 142
Cdd:cd17697   35 LEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNP 114
                         90       100       110
                 ....*....|....*....|....*....|
gi 568972939 143 QLLSEFYEPEA-LMMEEEGMVIVGLLVGLN 171
Cdd:cd17697  115 ELTGEWYYARSpFLSPELRSDILDSLYELN 144
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
555-607 7.92e-11

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 58.10  E-value: 7.92e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 555 EATHCKQCEKDF-----------SISRRKHHCRNCGHIFCNTCSSNELALPS--YPKPVRVCDSCH 607
Cdd:cd15718    5 ESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVmgFEFPVRVCNECY 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
249-556 1.90e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 249 KLQEEL-----SAATDRICSLQKEQQQLREQNEVIRERSEKSVEiTKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKK 323
Cdd:COG1196  217 ELKEELkeleaELLLLKLRELEAELEELEAELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 324 VrlelekelelqigmKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTT 403
Cdd:COG1196  296 E--------------LARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELE 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 404 QVMSSMKQMEERLQQAERARQAAEERSHKLQQELsgrgSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTs 483
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEEL----LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA- 429
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939 484 clLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEA 556
Cdd:COG1196  430 --LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
67-159 1.90e-10

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: 59.94  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  67 LKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIA--TSVRN------------LPELKTAVGRGRAWLYLALMQKKLA 132
Cdd:cd17689   38 LQHGLKTSRSPNLVSSAVTQVSGLAGSLGSAETEPTfwPFVKEhltkhelerfelLKNIWTDIGRGRAWLRSALNEHSLE 117
                         90       100
                 ....*....|....*....|....*..
gi 568972939 133 DYLKVLIDNKQLLSEFYEPEALMMEEE 159
Cdd:cd17689  118 RYLHILLSNENLLRQYYEDWAFLRDEE 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
244-546 2.14e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 244 EKTNSKL---QEELSAATDRICSLQKEQQQLREQneviRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKE 320
Cdd:COG1196  175 EEAERKLeatEENLERLEDILGELERQLEPLERQ----AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 321 EKKVRLELekelelqigmktemEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEG 400
Cdd:COG1196  251 LEAELEEL--------------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 401 KTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREK 480
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 481 DTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALK 546
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
290-547 2.17e-10

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: 63.93  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   290 KQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQiGMKTEMEIAMKLLEKDTHEKQ-----DTLVALR 364
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALL-KEKREYEGYELLKEKEALERQkeaieRQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   365 QQLEEVKAINLQMFHKVQSAESSLQQKNEAI-ASFEGKTTQVMSSMKQMEERLQQAERARQAAEERshklQQELSGRGSA 443
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE----LEDAEERLAK 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   444 LQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELR-ELQDEKAELRKVCEEQEQALQ 522
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdELKDYREKLEKLKREINELKR 406
                          250       260
                   ....*....|....*....|....*
gi 568972939   523 EMGLHLSQSKLKMEDIKEVNKALKG 547
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAG 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
223-545 2.24e-10

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: 63.93  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   223 EELNRHLSctvgDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEksveitkqdtkvELETYKQ 302
Cdd:TIGR02169  684 EGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE------------ELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   303 trqgldemysdvwkQLKEEkkvrlelekelelqigmKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQmfHKVQ 382
Cdd:TIGR02169  748 --------------SLEQE-----------------IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIP 794
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   383 SAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRdqcsglekEL 462
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE--------EL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   463 KSEKEQRQALQRELQREKdtscllqtelqqvEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVN 542
Cdd:TIGR02169  867 EEELEELEAALRDLESRL-------------GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933

                   ...
gi 568972939   543 KAL 545
Cdd:TIGR02169  934 SEI 936
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
550-606 3.24e-10

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 56.75  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 550 WLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCN----TCSSN--------------------ELALPSYPKPVRVCDS 605
Cdd:cd15737    2 WEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEvpldllssalpdlpfvfkepQSDIPDDTKSVRVCRD 81

                 .
gi 568972939 606 C 606
Cdd:cd15737   82 C 82
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
559-613 5.14e-10

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


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 55.71  E-value: 5.14e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939 559 CKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALpSYPK--PVRVCDSCHTLLLQR 613
Cdd:cd15742   12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYPL-KYLKdrPAKVCDGCFAELRKR 67
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
64-174 5.23e-10

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: 58.45  E-value: 5.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  64 EHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRA-------------------WLYL 124
Cdd:cd17687   31 DACLLHGLRKRALGLFRSSSTFSLLQKVAKSCPPAADILRKVQEIENLSENKRSSSSsgsnssnshgnsssnrkilWIRI 110
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 125 ALMQKKLADYLKVLIDNKqllSEFYEPEALMME-EEGMVIVGLLVGLNVLD 174
Cdd:cd17687  111 ALFEKVLDKIVDYLVENA---SKYYEKEALMADpVDGPLLASLLVGPCALD 158
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
333-546 8.21e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 8.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   333 ELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQM 412
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   413 EERLQQAERARQAAEERSHKLQQELsgrgSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQ 492
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939   493 VEGLKKELRE----LQDEKAELRKVCEEQEQAL-----------QEMGLHLSQSKLKMEDIKEVNKALK 546
Cdd:TIGR02168  843 LEEQIEELSEdiesLAAEIEELEELIEELESELeallnerasleEALALLRSELEELSEELRELESKRS 911
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
559-606 1.06e-09

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 54.50  E-value: 1.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568972939 559 CKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSYP------KPVRVCDSC 606
Cdd:cd15736    2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSAydprngKWYRCCHSC 55
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
558-606 1.12e-09

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: 54.43  E-value: 1.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 558 HCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNE--LALPSYPKPVRVCDSC 606
Cdd:cd15745    1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDlvLSVPDTCIYLRVCKTC 51
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
550-607 9.34e-09

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 52.38  E-value: 9.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 550 WLKDDEathCKQCEKDF-----------SISRRKHHCRNCGHIFCNTCSSNELALP--SYPKPVRVCDSCH 607
Cdd:cd15756    3 WLESDS---CQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPimGFEFQVRVCDSCF 70
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
34-170 1.04e-08

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: 54.17  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  34 SIKVLLQSALSLGRSLDADYAPLQQFFVVMEHCLKHGLKvkksfigQNKSFFGPLeLVEKLCPEASDiatSVRNLPELKT 113
Cdd:cd17680   12 SLQSYSSSQEEEDVLITNENRELQRLCEALDHALLHGLR-------RGNRGYWPF-VKEFTHKETIK---QIENLPNVTT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939 114 AVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALMMEEEGM-VIVGLLVGL 170
Cdd:cd17680   81 DLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLeLLLTLLSGL 138
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
355-537 2.00e-08

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: 56.70  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 355 EKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQ 434
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 435 QELSGRGSALQLQ------------------------LSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTsclLQTEL 490
Cdd:COG4942  104 EELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE---LEALL 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568972939 491 QQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMED 537
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
236-516 2.07e-08

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: 57.39  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   236 LQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREqnEVIRERSEKSVEITKQDTKVELETyKQTRQGLDEMYSDVW 315
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK--KIKDLGEEEQLRVKEKIGELEAEI-ASLERSIAEKERELE 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   316 KQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHE---KQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKN 392
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   393 EAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELsgrgSALQLQLSQLRDQCSGLEKELKSEKEQRQAL 472
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK----EDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 568972939   473 QRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEE 516
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
69-174 2.36e-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: 54.33  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  69 HGLKVKksfigQNKSFFGP-----LELVEKLCPEASDIATSVRN---LPELKTAVGRGRAWLYLALMQKKLADYLKVLID 140
Cdd:cd17677   65 HGLQTK-----QGKSALWShllayQENEERLKPLPESLLFDMKNvqnMKEIKTDVGYARAWIRLALEKKLLSKHLKTLLS 139
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568972939 141 NKQLLSEFYEPEA-LMMEEEGMVIVGLLVGLNVLD 174
Cdd:cd17677  140 NQDLLRSLYKRYAfLRCEDEREQFLYHLLSLNAVD 174
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
251-523 2.62e-08

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: 57.27  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  251 QEELSAATDRIcslqKEQQQLREQNEVIRERSEKSVEITKQDT---KVELETYKQtrqGLDEM------YSDVWKQLKEE 321
Cdd:COG3096   353 QEDLEELTERL----EEQEEVVEEAAEQLAEAEARLEAAEEEVdslKSQLADYQQ---ALDVQqtraiqYQQAVQALEKA 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  322 KKVrlelekelelqigmktemeiaMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGK 401
Cdd:COG3096   426 RAL---------------------CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKI 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  402 TTQVmssmkqmeERLQQAERARQAAEErsHKLQQELSGRGSALQLQLSQLRDqcsgLEKELKSEKEQRQALQRELQREKD 481
Cdd:COG3096   485 AGEV--------ERSQAWQTARELLRR--YRSQQALAQRLQQLRAQLAELEQ----RLRQQQNAERLLEEFCQRIGQQLD 550
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568972939  482 TSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:COG3096   551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
559-607 2.66e-08

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: 50.20  E-value: 2.66e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568972939 559 CKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALPSY-PKPVRVCDSCH 607
Cdd:cd15749    2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKgNQKQKVCKQCH 51
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
216-524 2.72e-08

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: 57.06  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  216 LDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLR----EQNEVIRERSEKSVEITKQ 291
Cdd:pfam17380 236 MERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfekmEQERLRQEKEEKAREVERR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  292 DTKVELETYKQT---RQG--LDEMYSDVWKQLKEEKKVRLELEKELELQIGMKT-EMEIA-MKLLEKDTHEKQDTLVALR 364
Cdd:pfam17380 316 RKLEEAEKARQAemdRQAaiYAEQERMAMERERELERIRQEERKRELERIRQEEiAMEISrMRELERLQMERQQKNERVR 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  365 QQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKqmEERLQQAERARQAAEERSHKL----QQELSGR 440
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREMERVRLEEQERQQQVerlrQQEEERK 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  441 GSALQLQLSQlrdqcsglEKELKSEKEQRQALQRELQREKDTsclLQTELQQVEGLKKELRELQDEKAE--LRKVCEEQE 518
Cdd:pfam17380 474 RKKLELEKEK--------RDRKRAEEQRRKILEKELEERKQA---MIEEERKRKLLEKEMEERQKAIYEeeRRREAEEER 542

                  ....*.
gi 568972939  519 QALQEM 524
Cdd:pfam17380 543 RKQQEM 548
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-500 3.31e-08

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: 57.00  E-value: 3.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   204 DSGREHERITDVLDQKNyvEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSE 283
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   284 KSVEitkqdtkvELETYKQTRQGLDEMYSDvwKQLKEEKKVRLELEKELELQIgMKTEMEIAMKLLEKDTHEKQDTLVAL 363
Cdd:TIGR02169  340 ELER--------EIEEERKRRDKLTEEYAE--LKEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREINELKREL 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   364 RQQLEEVkainlqmfhkvQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSgrgsA 443
Cdd:TIGR02169  409 DRLQEEL-----------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY----D 473
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939   444 LQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKEL 500
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
550-607 3.65e-08

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 50.45  E-value: 3.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 550 WLKDDEathCKQCEKDF-----------SISRRKHHCRNCGHIFCNTCSSNELALP--SYPKPVRVCDSCH 607
Cdd:cd15757    3 WLDSDS---CQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSKRSTIPlmGFEFEVRVCDSCH 70
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
251-480 4.44e-08

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: 56.29  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  251 QEELSAATDRICSLQKEQQQLREQNEVIRErseksveitkqdtkvELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEK 330
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQ---------------ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  331 ELELQIG-MKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSA-----------ESSLQQKNEAIASF 398
Cdd:pfam17380 432 ARQREVRrLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrrkilEKELEERKQAMIEE 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  399 EGKTTQVMSSMKQMEERLQQAERARQAAEERshKLQQELSGRgSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQR 478
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEERRREAEEER--RKQQEMEER-RRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588

                  ..
gi 568972939  479 EK 480
Cdd:pfam17380 589 AE 590
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
267-540 4.86e-08

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: 56.23  E-value: 4.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   267 EQQQLREQNEVIRERSEKsVEITKQDTKVELETYKQTRQGLdEMYSDVWKQLKE-EKKVRLELEKELELQIgMKTEMEIA 345
Cdd:TIGR02169  171 KKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKA-ERYQALLKEKREyEGYELLKEKEALERQK-EAIERQLA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   346 -----MKLLEKDTHEKQDTLVALRQQLEEvkaINLQMfhKVQSAESSLQQKNEaIASFEGKTTQVMSSMKQMEERLQQAE 420
Cdd:TIGR02169  248 sleeeLEKLTEEISELEKRLEEIEQLLEE---LNKKI--KDLGEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   421 RARQAAEERSHKLQQE---LSGRGSALQLQLSQL----------------------------RDQCSGLEKELKSEKEQR 469
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLteeyaelkeeledlraeleevdkefaetRDELKDYREKLEKLKREI 401
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568972939   470 QALQRELQREKDTSCLLQTEL----QQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKE 540
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELadlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
199-524 8.21e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 8.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 199 DAQDLDSGREHERiTDVLDQKNYVEELN---RHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEqqqLREQN 275
Cdd:PRK02224 364 EAAELESELEEAR-EAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT---LRTAR 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 276 EVIRErSEKSVEITK-----QDTK----VE-LETYKQTRQGLDEMYSDVWKQLKE-EKKV-RLELEKELELQIG-MKTEM 342
Cdd:PRK02224 440 ERVEE-AEALLEAGKcpecgQPVEgsphVEtIEEDRERVEELEAELEDLEEEVEEvEERLeRAEDLVEAEDRIErLEERR 518
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 343 EIAMKLL---EKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQME---ERL 416
Cdd:PRK02224 519 EDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirTLL 598
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 417 QQAERARQAAEERSHKLQQeLSGRGSALQLQLSQLRDQCSGLE--------KELKSEKEQRQALQ-------RELQREKD 481
Cdd:PRK02224 599 AAIADAEDEIERLREKREA-LAELNDERRERLAEKRERKRELEaefdeariEEAREDKERAEEYLeqveeklDELREERD 677
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568972939 482 TsclLQTELQQVEGLKKELRELQDEKAELRKVCE------EQEQALQEM 524
Cdd:PRK02224 678 D---LQAEIGAVENELEELEELRERREALENRVEalealyDEAEELESM 723
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
350-531 1.02e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  350 EKDTHEKQDTLVALRQQLEEvkainlqMFHKVQSAESSLQQKNEAIASFEgkttqvmsSMKQMEERLQQAERARQA---- 425
Cdd:COG4913   220 EPDTFEAADALVEHFDDLER-------AHEALEDAREQIELLEPIRELAE--------RYAAARERLAELEYLRAAlrlw 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  426 -AEERSHKLQQELSgrgsALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQrekdtscllQTELQQVEGLKKELRELQ 504
Cdd:COG4913   285 fAQRRLELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351
                         170       180
                  ....*....|....*....|....*..
gi 568972939  505 DEKAELRKVCEEQEQALQEMGLHLSQS 531
Cdd:COG4913   352 RELEERERRRARLEALLAALGLPLPAS 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
413-538 1.04e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  413 EERLQQAERARQAAEERSHKLQQELSgrgsalqlQLSQLRDQCSGL------EKELKSEKEQRQALQRELQREKDTSCLL 486
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELD--------ALQERREALQRLaeyswdEIDVASAEREIAELEAELERLDASSDDL 687
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568972939  487 QTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDI 538
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-539 1.73e-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: 54.68  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   272 REQNEVIRERSEKSVEITKQDTKVElETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEK 351
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELE-EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   352 DTHEkqdtlvaLRQQLEEVKAINLQMfhkvQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSH 431
Cdd:TIGR02168  745 LEER-------IAQLSKELTELEAEI----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   432 KLQQELSGRGSA-----------------LQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDtscLLQTELQQVE 494
Cdd:TIGR02168  814 LLNEEAANLRERleslerriaaterrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN---ERASLEEALA 890
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 568972939   495 GLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIK 539
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
558-609 1.73e-07

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


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 47.74  E-value: 1.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568972939 558 HCKQCEKDFSISRRKHHCRNCGHIFCNTCSSNElalpsyPKPVRVCDSCHTL 609
Cdd:cd15750    2 PCESCGAKFSVFKRKRTCADCKRYFCSNCLSKE------ERGRRRCRRCRAL 47
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
105-174 1.86e-07

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: 51.98  E-value: 1.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 105 VRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEA-LMMEEEGMVIVGLLVGLNVLD 174
Cdd:cd17691  127 IQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAfLRCEEEKEQFLYHLLSLNAVD 197
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
56-153 3.08e-07

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: 50.34  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  56 LQQFFVVMEHCLKHGLKVKKSFIGQNkSFFGPLELVEKLCPEASDIATSVRNLPELKTAVG-RGRAWLYLALMQKKLADY 134
Cdd:cd17686   21 LQRLCRAVENILQHGLKEFQGLNKEI-DDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEVSdKGRLWLRQSLQQHCLSSQ 99
                         90
                 ....*....|....*....
gi 568972939 135 LKVLIDNKQLLSEFYEPEA 153
Cdd:cd17686  100 LQWLVSDKELLRKYYEDEA 118
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
233-536 9.16e-07

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: 52.10  E-value: 9.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   233 VGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQN-EVIRER-------SEKSVEITKQDTKVELETYKQTR 304
Cdd:pfam01576  105 IQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNsKLSKERklleeriSEFTSNLAEEEEKAKSLSKLKNK 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   305 QglDEMYSDVWKQLKEEKKVRLelekelelqigmktEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSA 384
Cdd:pfam01576  185 H--EAMISDLEERLKKEEKGRQ--------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAA 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   385 ESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELsgrgSALQLQLSQLRDQcSGLEKELKS 464
Cdd:pfam01576  249 LARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL----EALKTELEDTLDT-TAAQQELRS 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   465 EKEQRQA-LQRELQREKDT-----SCLLQTELQQVEGLKKELRELQDEKAELRK---VCEEQEQALQEMGLHLSQSKLKM 535
Cdd:pfam01576  324 KREQEVTeLKKALEEETRSheaqlQEMRQKHTQALEELTEQLEQAKRNKANLEKakqALESENAELQAELRTLQQAKQDS 403

                   .
gi 568972939   536 E 536
Cdd:pfam01576  404 E 404
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
559-610 9.76e-07

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


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 46.34  E-value: 9.76e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939 559 CKQCEKDFS-ISRRKHHCRNCGHIFCNTCSSNEL--------ALPSYPKPVRVCDSCHTLL 610
Cdd:cd15723    2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVprsvmgatAPAAQRETVFVCSGCNDKL 62
PTZ00121 PTZ00121
MAEBL; Provisional
249-541 1.06e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  249 KLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITK---QDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVR 325
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  326 LElekelelQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAInlqmfHKVQSAESSLQQKNEAIAsfegkttqv 405
Cdd:PTZ00121 1609 AE-------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-----EELKKAEEENKIKAAEEA--------- 1667
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  406 mssmKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQL-QLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSC 484
Cdd:PTZ00121 1668 ----KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939  485 LLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEV 541
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
552-606 1.10e-06

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


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 45.76  E-value: 1.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 552 KDDEATHCKQCEKDF-SISRRKHHCRNCGHIFCNTCSSNElalPSYPKPVRVCDSC 606
Cdd:cd15740    1 REKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCSEFK---DLASRHNRVCRDC 53
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
223-546 1.16e-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: 51.56  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  223 EELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLR-EQNEVIRERSEKSVEITKQDTKV-----E 296
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdEQNKIKKQLSEKQKELEQNNKKIkelekQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  297 LETYKQTRQGLDEMYSDVW-KQLKEEKKVRLELEKELELQIGMK----TEMEIAMKLLEKDTHEKQDTLVALRQQLEEVK 371
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNnkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQ 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  372 AINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERshklQQELSGRGSALQLQLSQL 451
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE----IERLKETIIKNNSEIKDL 445
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  452 RDQCSGLEKELKSEKEQRQALQRELqreKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQS 531
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
                         330
                  ....*....|....*....
gi 568972939  532 KLKMED----IKEVNKALK 546
Cdd:TIGR04523 523 KEKIEKleseKKEKESKIS 541
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
254-535 1.92e-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: 50.53  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 254 LSAATDRICSLQKEQQQLREQneviRERSEKSVEITKQDTKVELETYKQTRQGLDEMysdvwkqlkeEKKVRlelekele 333
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAAL----------ARRIR-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 334 lqigmKTEMEIAmkLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSaeSSLQQKNEAIASFEGKTTQVMSSM---K 410
Cdd:COG4942   73 -----ALEQELA--ALEAELAELEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSPEDFLDAVRRLQylkY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 411 QMEERLQQAERARQAAEERShKLQQELSGRGSALQLQLSQLRDQcsglEKELKSEKEQRQALQRELQREKdtscllQTEL 490
Cdd:COG4942  144 LAPARREQAEELRADLAELA-ALRAELEAERAELEALLAELEEE----RAALEALKAERQKLLARLEKEL------AELA 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568972939 491 QQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKM 535
Cdd:COG4942  213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
209-546 2.10e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 209 HERITDVLDQKNYVEELNRHLSC-TVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEK--- 284
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpv 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 285 -SVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVAL 363
Cdd:PRK03918 441 cGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL 520
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 364 RQQLEEVKAINlQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERArqaAEERSHKLQQELSGRGSA 443
Cdd:PRK03918 521 EKKAEEYEKLK-EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKE 596
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 444 LQ------LQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQV---------EGLKKELRELQDEKA 508
Cdd:PRK03918 597 LEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyEELREEYLELSRELA 676
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568972939 509 ELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALK 546
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
548-606 2.80e-06

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


Pssm-ID: 277300  Cd Length: 76  Bit Score: 45.34  E-value: 2.80e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 548 HTWLKDDEATHCKQCEKDFSISRRKHHCRNCGHIFCNTCSSN--ELALPSYPKPV-----RVCDSC 606
Cdd:cd15761    2 SHWKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNriKLNNSAEYDPKngkwcRCCEKC 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
309-546 3.66e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 309 EMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqMFHKVQSAESSL 388
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKEL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 389 QQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQ---------QELSGRGSALQLQLSQLRDQCSGLE 459
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelkelKEKAEEYIKLSEFYEEYLDELREIE 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 460 KELKSEKEQRQALQRELQRekdtsclLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMG-LHLSQSKLKMEDI 538
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKE-------LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEeLERLKKRLTGLTP 386

                 ....*...
gi 568972939 539 KEVNKALK 546
Cdd:PRK03918 387 EKLEKELE 394
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
201-491 3.68e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 49.68  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  201 QDLDSGREHERItDVLDQKNYVEELNRHLSCTVGDLQTkidgLEKTNSKLQEELSAATDRICSLQKEQQQLREQ------ 274
Cdd:pfam19220 100 REAEAAKEELRI-ELRDKTAQAEALERQLAAETEQNRA----LEEENKALREEAQAAEKALQRAEGELATARERlalleq 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  275 -NEVIRERSEK-SVEITKQDTKV-ELET-YKQTRQGLDEMYSdvwkQLKEEKKVRLELEKELELQIG-MKTEME-IAMKL 348
Cdd:pfam19220 175 eNRRLQALSEEqAAELAELTRRLaELETqLDATRARLRALEG----QLAAEQAERERAEAQLEEAVEaHRAERAsLRMKL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  349 --LEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAA 426
Cdd:pfam19220 251 eaLTARAAATEQLLAEARNQLRDRDE-------AIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAEL 323
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972939  427 EERSHKLQQELSGRGSALQ---LQLSQLRDQCSGLEKELKSEK---EQR-QALQRELQREKDTSCLLQTELQ 491
Cdd:pfam19220 324 EERAEMLTKALAAKDAALEraeERIASLSDRIAELTKRFEVERaalEQAnRRLKEELQRERAERALAQGALE 395
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-548 4.35e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 219 KNYVEELNRHLSCTvGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVE-- 296
Cdd:PRK03918 175 KRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEgs 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 297 LETYKQTRQGLDEMYSDVWKQLKE-EKKVRLELEKElelqiGMKTEMEIAMKLLEKDTHEKQD---TLVALRQQLEEVKA 372
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEElEEKVKELKELK-----EKAEEYIKLSEFYEEYLDELREiekRLSRLEEEINGIEE 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 373 inlqmfhKVQSAESslqqKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAE--------------ERSHKLQQELS 438
Cdd:PRK03918 329 -------RIKELEE----KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELE 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 439 GRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQ----------RELQrEKDTSCLLQTELQQVEGLKKELRELQDEKA 508
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELT-EEHRKELLEEYTAELKRIEKELKEIEEKER 476
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 568972939 509 ELRKVCEEQEQALQEMGLHLSQSKLkMEDIKEVNKALKGH 548
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKY 515
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
343-515 4.58e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  343 EIAMKLLEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTtqvmssMKQMEERLQQAERA 422
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEA-------RLDALREELDELEAQIRGNGGDR------LEQLEREIERLERE 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  423 RQAAEERSHKLQQELSGRG----------SALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTsclLQTELQQ 492
Cdd:COG4913   354 LEERERRRARLEALLAALGlplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE---LEAEIAS 430
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568972939  493 VEG-----------LKKEL-RELQDEKAELRKVCE 515
Cdd:COG4913   431 LERrksniparllaLRDALaEALGLDEAELPFVGE 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
232-546 6.48e-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: 49.25  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  232 TVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNevirerseKSVEITKQDTKVELETYKQTRQGLDEMY 311
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI--------KNLESQINDLESKIQNQEKLNQQKDEQI 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  312 sdvwKQLKEEKKVRLELEKELELQIgMKTEMEIamKLLEKDTHEKQ---DTLVALRQQLEE-VKAINLQmfhkVQSAESS 387
Cdd:TIGR04523 415 ----KKLQQEKELLEKEIERLKETI-IKNNSEI--KDLTNQDSVKEliiKNLDNTRESLETqLKVLSRS----INKIKQN 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  388 LQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERshklQQELSGRGSALQLQLSQLRDQCSGLEKELKSE-- 465
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKEnl 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  466 KEQRQALQRELQREKDTSCLLQTELQQvegLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKAL 545
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKSLKKKQEE---KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636

                  .
gi 568972939  546 K 546
Cdd:TIGR04523 637 K 637
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
349-523 7.09e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 349 LEKDTHEKQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLqqAERARQAAE- 427
Cdd:COG3883   28 LQAELEAAQAELDALQAELEELNE-------EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRs 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 428 --------------------ERSHKLQQeLSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTsclLQ 487
Cdd:COG3883   99 ggsvsyldvllgsesfsdflDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE---LE 174
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568972939 488 TELQQVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
350-540 1.23e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 350 EKDTHekqDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQ---VMSSMKQMEERLQQAERARQAA 426
Cdd:PRK02224 201 EKDLH---ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREEL 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 427 EERSHKLQQELSGRGSALqlqlSQLRDQCSGLEKELKSEKEQRQALQR---ELQREKDTSCL-LQTELQQVEGLKKELRE 502
Cdd:PRK02224 278 AEEVRDLRERLEELEEER----DDLLAEAGLDDADAEAVEARREELEDrdeELRDRLEECRVaAQAHNEEAESLREDADD 353
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568972939 503 LQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKE 540
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
COG5022 COG5022
Myosin heavy chain [General function prediction only];
366-573 1.31e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  366 QLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQvmSSMKQMEERLQQAERaRQAAEERSHKLQQElSGRGSALQ 445
Cdd:COG5022   823 QKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRF--SLLKKETIYLQSAQR-VELAERQLQELKID-VKSISSLK 898
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  446 LQLSQLRDQCSGLEKELKSE-------KEQRQALQRELQREKDTSCLLQTELQQveglKKELRELQDEKAELRKVCEEQE 518
Cdd:COG5022   899 LVNLELESEIIELKKSLSSDlienlefKTELIARLKKLLNNIDLEEGPSIEYVK----LPELNKLHEVESKLKETSEEYE 974
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568972939  519 QALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEATHCKQCEKDFSISRRKH 573
Cdd:COG5022   975 DLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQ 1029
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
224-546 1.50e-05

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: 48.18  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  224 ELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQ-QLREQNeviRERSEKSVEITKQDTKV-ELETYK 301
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaQMEELN---KAKAAHSFVVTEFEATTcSLEELL 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  302 QTRQGLDEMYSDVWKQLKEEKKVRLELEKELELqigMKTEMEIAMKLLEKDTHEKQdTLVALRQQLEEVKAinlQMFHKV 381
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTK---FKNNKEVELEELKKILAEDE-KLLDEKKQFEKIAE---ELKGKE 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  382 QSAESSLQQKNEAIASFEGKTTQVMSSmkqMEERLQQAERARQAAEERSHKlQQELSGRGSALQLQLSQLRDQCSGLEKE 461
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTS---EEHYLKEVEDLKTELEKEKLK-NIELTAHCDKLLLENKELTQEASDMTLE 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  462 LKSEKEQRQALQRELQRE-KDTSCLLQTELQ---QVEGLKKELRELQDE-KAELRKVCEEQEQALQEMGLHLSQSKLKME 536
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMlKQIENLEEKEMNlrdELESVREEFIQKGDEvKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
                         330
                  ....*....|
gi 568972939  537 DIKEVNKALK 546
Cdd:pfam05483 595 KCNNLKKQIE 604
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
409-541 1.60e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 409 MKQMEERLQQAERARQAAEERSHKLQQElsgrgsalqlQLSQLRDqcsglekELKSEKEQRQALQRELQREKDtscllqt 488
Cdd:COG0542  413 LDELERRLEQLEIEKEALKKEQDEASFE----------RLAELRD-------ELAELEEELEALKARWEAEKE------- 468
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568972939 489 ELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGlHLSQSKLKMEDIKEV 541
Cdd:COG0542  469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELA-PLLREEVTEEDIAEV 520
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
357-546 1.79e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 357 QDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQE 436
Cdd:COG3883   15 DPQIQAKQKELSELQA-------ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 437 LSGRGSALQLQLSQLrdqcSGLEKELKSEK-----EQRQALQRELQREKDTSCLLQTELQQVEGLKKELrelQDEKAELR 511
Cdd:COG3883   88 LGERARALYRSGGSV----SYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAEL---EAKLAELE 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568972939 512 KVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALK 546
Cdd:COG3883  161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
365-523 2.01e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 365 QQLEEVKainlQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAE--ERSHKLQQELSGRGS 442
Cdd:COG4717   71 KELKELE----EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 443 ALQ------LQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSclLQTELQQVEGLKKELRELQDEKAELRKVCEE 516
Cdd:COG4717  147 RLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELEEAQEELEE 224

                 ....*..
gi 568972939 517 QEQALQE 523
Cdd:COG4717  225 LEEELEQ 231
FYVE_CARP1 cd15769
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ...
559-609 2.21e-05

FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is 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, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain.


Pssm-ID: 277308  Cd Length: 47  Bit Score: 41.90  E-value: 2.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 559 CKQCEKDFSISRRKHHCRNCGHIFCNTCSSNELALpsypkpvRVCDSCHTL 609
Cdd:cd15769    4 CKACGLAFSVFRKKHVCCDCKKDFCSVCSVLQENL-------RRCSTCHLL 47
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
349-507 2.35e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 349 LEKDTHEKQDTLVALRQQLEEVKAI--NLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAA 426
Cdd:COG4717   93 LQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 427 EERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKdtscllqtelQQVEGLKKELRELQDE 506
Cdd:COG4717  173 AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE----------EELEQLENELEAAALE 242

                 .
gi 568972939 507 K 507
Cdd:COG4717  243 E 243
RUN_SGSM1 cd17703
RUN domain found in small G protein signaling modulator 1 (SGSM1) and similar proteins; SGSM1, ...
52-169 3.01e-05

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: 45.00  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  52 DYAPLQQFFVVMEHCLKHGL-----------KVKKSFIGQNKSFfgplELVEKLCPEASD--------------IATSVR 106
Cdd:cd17703   19 DSSHIISFCAAVEACVLHGLkrraagflrsnKIAALFMKVGKSF----PPAEELCRKVQEleqllenkrnqmqgLQENVR 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 107 NLPELKTAVGRG--RAWLYLALMQKKLADYLKVLIDNKqllSEFYEPEALMMEE-EGMVIVGLLVG 169
Cdd:cd17703   95 KMPKLPNLSPQAikHLWIRTALFEKVLDKIVHYLVENS---SKYYEKEALLMDPvDGPILASLLVG 157
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
257-548 3.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  257 ATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQdtkveLETYKQTRQGLDEMYSDV--WKQLKEEkkvrlelekelel 334
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA-----LQERREALQRLAEYSWDEidVASAERE------------- 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  335 qIgmkTEMEIAMKLLEKDthekQDTLVALRQQLEEVKAinlqmfhKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEE 414
Cdd:COG4913   670 -I---AELEAELERLDAS----SDDLAALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  415 RLQQAERA-----RQAAEERSHKLQQELSGR--GSALQLQLSQLRDQCSGLEKELksekeqRQALQRELQREKDTSCLLQ 487
Cdd:COG4913   735 RLEAAEDLarlelRALLEERFAAALGDAVERelRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLD 808
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972939  488 TELQQVEGLKKELRELQDE-----KAELRKVCEEQEQALQEmglHLsQSKLKME--DIKE----VNKALKGH 548
Cdd:COG4913   809 ADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVA---DL-LSKLRRAirEIKEridpLNDSLKRI 876
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
541-607 3.89e-05

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 47.00  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  541 VNKALKGHTWLKDDEAT-HCKQCEKDF-SISR----RKHHCRNCGHIFCNTC-------SSNELALPSYPKPVR---VCD 604
Cdd:PTZ00303  444 LTKLLHNPSWQKDDESSdSCPSCGRAFiSLSRplgtRAHHCRSCGIRLCVFCitkrahySFAKLAKPGSSDEAEerlVCD 523

                  ...
gi 568972939  605 SCH 607
Cdd:PTZ00303  524 TCY 526
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
354-523 4.58e-05

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: 45.30  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 354 HEKQDTLVALRQQLEEVKAINlqmfHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKL 433
Cdd:COG1579    3 PEDLRALLDLQELDSELDRLE----HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 434 QQELSGRGS-----ALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEG-LKKELRELQDEK 507
Cdd:COG1579   79 EEQLGNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAEL 158
                        170
                 ....*....|....*.
gi 568972939 508 AELRKVCEEQEQALQE 523
Cdd:COG1579  159 EELEAEREELAAKIPP 174
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
197-536 5.39e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 46.04  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  197 LKDAQDLDSGREHERITDVLDQKNYvEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNE 276
Cdd:pfam07888  47 LQAQEAANRQREKEKERYKRDREQW-ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  277 V----IRERSEKSVEIT--KQDTKVELETYKQTRQGLDemysdvwKQLKEE----KKVRLELEKELELQIGMKTEMEIAM 346
Cdd:pfam07888 126 AhearIRELEEDIKTLTqrVLERETELERMKERAKKAG-------AQRKEEeaerKQLQAKLQQTEEELRSLSKEFQELR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  347 KLL-EKDTH--EKQDTLVALRQQLEEVK---AINLQMFHKVQSAESSL---QQKNEAI----ASFEGKTTQVMSSMKQMe 413
Cdd:pfam07888 199 NSLaQRDTQvlQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQERLnasERKVEGLgeelSSMAAQRDRTQAELHQA- 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  414 eRLQQAERARQAA-------EERSHKLQQELSGRGSAL--QLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSc 484
Cdd:pfam07888 278 -RLQAAQLTLQLAdaslalrEGRARWAQERETLQQSAEadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCN- 355
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568972939  485 llqteLQQVEGLKKELRELqdeKAELRKVCEEQEQAL---QEMGLHLSQSKLKME 536
Cdd:pfam07888 356 -----RVQLSESRRELQEL---KASLRVAQKEKEQLQaekQELLEYIRQLEQRLE 402
PRK11281 PRK11281
mechanosensitive channel MscK;
347-523 7.28e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  347 KLLEKDTHEKQDTLvalrQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMS------SMKQMEERLQQAE 420
Cdd:PRK11281   59 KLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRetlstlSLRQLESRLAQTL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  421 RARQAAEE--------------RSHKLQQELSgrgSALQlQLSQLRDQCSGLEKELKSEK-EQRQALQRELQREKDTSCL 485
Cdd:PRK11281  135 DQLQNAQNdlaeynsqlvslqtQPERAQAALY---ANSQ-RLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNAQNDL 210
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568972939  486 LQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:PRK11281  211 QRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
46 PHA02562
endonuclease subunit; Provisional
262-512 8.11e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.78  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 262 CSLQKE--QQQLREQNEVIRERSEKSveitkqdtkveletyKQTRQGLDEMYSDvwkqLKEEKKVRLELEKELELQIgmk 339
Cdd:PHA02562 186 LDMKIDhiQQQIKTYNKNIEEQRKKN---------------GENIARKQNKYDE----LVEEAKTIKAEIEELTDEL--- 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 340 TEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAInLQMFHKVQSAESSLQQkneaIASFEGKTTQVMSSMKQMEERLQQA 419
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGVCPTCTQQ----ISEGPDRITKIKDKLKELQHSLEKL 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 420 ERARQAAEERSHKLQqELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDtscllqtelqQVEGLKKE 499
Cdd:PHA02562 319 DTAIDELEEIMDEFN-EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE----------ELAKLQDE 387
                        250
                 ....*....|...
gi 568972939 500 LRELQDEKAELRK 512
Cdd:PHA02562 388 LDKIVKTKSELVK 400
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
358-515 8.33e-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: 45.71  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  358 DTLVALRQQLEEVKainlQMFHKVQSAESSL----QQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKL 433
Cdd:COG3096   512 QRLQQLRAQLAELE----QRLRQQQNAERLLeefcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  434 QQ------ELSGRGSA---LQLQLSQLRDQCSgleKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQ 504
Cdd:COG3096   588 EQlrarikELAARAPAwlaAQDALERLREQSG---EALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
                         170
                  ....*....|....*
gi 568972939  505 ----DEKAELRKVCE 515
Cdd:COG3096   665 qpggAEDPRLLALAE 679
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
362-498 8.77e-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: 45.71  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  362 ALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAE-RARQAAEERSHKLQQELSGr 440
Cdd:COG3096   988 KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGvQADAEAEERARIRRDELHE- 1066
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939  441 gsalqlQLSQLRDQCSGLEKELKS-EKEQRQALQRELQREKDtsclLQTELQQVEGLKK 498
Cdd:COG3096  1067 ------ELSQNRSRRSQLEKQLTRcEAEMDSLQKRLRKAERD----YKQEREQVVQAKA 1115
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
337-523 1.13e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  337 GMKTEMEIA---MKLLE--KDTHEKQDTLVALRQQLEEVKAInlqmfHKVQSAESSLQQKNEAIASFEgkttqvmSSMKQ 411
Cdd:COG4913   239 RAHEALEDAreqIELLEpiRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELR-------AELAR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  412 MEERLQQAERARQAAEERSHKLQQELSGRGSAlqlQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKdtscllqtelQ 491
Cdd:COG4913   307 LEAELERLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALG----------L 373
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568972939  492 QVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
208-510 1.55e-04

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: 44.81  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  208 EHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSA----ATDRICSLQ-KEQQQLREQNEviRERS 282
Cdd:pfam10174  51 EAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTspvdGEDKFSTPElTEENFRRLQSE--HERQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  283 EKSVEI---TKQDTKVELETYKQTRQGLDEMYSDVWK--QLKEEKKVRLELEKELELQIGmktEMEIAMKLLEKDTHEKQ 357
Cdd:pfam10174 129 AKELFLlrkTLEEMELRIETQKQTLGARDESIKKLLEmlQSKGLPKKSGEEDWERTRRIA---EAEMQLGHLEVLLDQKE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  358 DTLVALRQQLEEvKAINLQMFHKVQSAESSLQQKNEAIASFEGKT-----------TQVMSSMKQMEERLQQAERARQAA 426
Cdd:pfam10174 206 KENIHLREELHR-RNQLQPDPAKTKALQTVIEMKDTKISSLERNIrdledevqmlkTNGLLHTEDREEEIKQMEVYKSHS 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  427 EERSHK---LQQELSGRGS---ALQLQLSQLRDQCSGLE------KELKSEKEQRQALqreLQREKDTSCLLQTELQQVE 494
Cdd:pfam10174 285 KFMKNKidqLKQELSKKESellALQTKLETLTNQNSDCKqhievlKESLTAKEQRAAI---LQTEVDALRLRLEEKESFL 361
                         330
                  ....*....|....*..
gi 568972939  495 GLK-KELRELQDEKAEL 510
Cdd:pfam10174 362 NKKtKQLQDLTEEKSTL 378
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
223-545 1.55e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 223 EELNRhLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEViRERSEKSVEITKQDTKVELEtykQ 302
Cdd:PRK02224 251 EELET-LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL-DDADAEAVEARREELEDRDE---E 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 303 TRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKT---EMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFH 379
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 380 KVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERAR---------QAAEERSH-KLQQELSGRGSALQLQLS 449
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHvETIEEDRERVEELEAELE 485
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 450 QLRDQCSGLEKEL---KSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMgl 526
Cdd:PRK02224 486 DLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-- 563
                        330
                 ....*....|....*....
gi 568972939 527 hLSQSKLKMEDIKEVNKAL 545
Cdd:PRK02224 564 -EEEAEEAREEVAELNSKL 581
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
215-517 1.95e-04

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: 44.71  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  215 VLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATdriCSLQKEQQQLREQNEVIRERSEKSVEITKQDTK 294
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK---TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  295 VELETYKQTRQGldemySDVWKQLKEEKKvrlelekeleLQIGMKTEMEIAMKLLEKdtheKQDTLVALRQQLEEVKAin 374
Cdd:pfam05483 497 LLLENKELTQEA-----SDMTLELKKHQE----------DIINCKKQEERMLKQIEN----LEEKEMNLRDELESVRE-- 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  375 lQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQE---LSGRGSALQLQLSQL 451
Cdd:pfam05483 556 -EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAY 634
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568972939  452 RDQCSGLEKELKSEKEQRQALQRELQRE-KDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQ 517
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHK 701
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
210-435 2.19e-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: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 210 ERITDVLDQ--KNYVEElnrhlsctvgDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVE 287
Cdd:COG3206  148 ELAAAVANAlaEAYLEQ----------NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLL 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 288 ITK-QDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTH--EKQDTLVALR 364
Cdd:COG3206  218 LQQlSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytPNHPDVIALR 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939 365 QQLEEVKA--------INLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQ 435
Cdd:COG3206  298 AQIAALRAqlqqeaqrILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
238-522 2.68e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  238 TKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQ-NEVIRERSEKSVEITKQDTKVELetykqtrqgLDEMYSDVWK 316
Cdd:TIGR04523  96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQkKENKKNIDKFLTEIKKKEKELEK---------LNNKYNDLKK 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  317 QLKEEKKVRLELEKELE--LQIGMKTEMEIAMKLLE----KDTHEKQDTLVAlrqQLEEVKAINLQMFHKVQSAESSLQQ 390
Cdd:TIGR04523 167 QKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLlsnlKKKIQKNKSLES---QISELKKQNNQLKDNIEKKQQEINE 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  391 KNEAIASFEGKTTQVMSSMKQMEERLQQaeraRQAAEERSHKLQQELSGRGSALQLQLSQLRDQ-CSGLEKELKSEKEQR 469
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQ 319
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568972939  470 QALQRELQREKDTSCLLQTEL-QQVEGLKKELRELQDEKAELRKVCEEQEQALQ 522
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLnEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
PTZ00121 PTZ00121
MAEBL; Provisional
244-564 2.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  244 EKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVEletykQTRQGLDEMYSDVWKQLKEEKK 323
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE-----EDKKKADELKKAAAAKKKADEA 1423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  324 VRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQmfHKVQSAESSLQQKNEAiasfeGKTT 403
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKA-----EEAK 1496
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  404 QVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEK--ELKSEKEQRQALQRELQREKD 481
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDK 1576
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  482 TSCLLQTE-LQQVEglKKELRELQDEKAELRKVCEEQEQALQEmglhlsqSKLKMEDIKEVNKALKGHTWLKDDEATHCK 560
Cdd:PTZ00121 1577 NMALRKAEeAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEE-------AKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647

                  ....
gi 568972939  561 QCEK 564
Cdd:PTZ00121 1648 KAEE 1651
PTZ00121 PTZ00121
MAEBL; Provisional
249-564 3.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  249 KLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDtkvELETYKQTRQGLDEMYSDVWKQLKEEKKVRLEL 328
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD---EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  329 EKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVK-AINLQMFHKVQSAESsLQQKNEAIASFEGKTTQVMS 407
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkADEAKKAEEAKKADE-AKKAEEAKKADEAKKAEEKK 1546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  408 SMKQME--ERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLR---------DQCSGLEKELKSEKEQR---QALQ 473
Cdd:PTZ00121 1547 KADELKkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAEEAKKAEEAKikaEELK 1626
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  474 RELQREKDTSCLLQTELQQV---EGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTW 550
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
                         330
                  ....*....|....
gi 568972939  551 LKDDEATHCKQCEK 564
Cdd:PTZ00121 1707 LKKKEAEEKKKAEE 1720
PTZ00121 PTZ00121
MAEBL; Provisional
265-565 3.81e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  265 QKEQQQLREQNEVIR-ERSEKSVEITKQDtkvELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKtEME 343
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKaDEAKKAEEAKKAD---EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAE 1584
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  344 IAMKLLEKDTHEkqdtlvaLRQQLEEVKAINLQMFHKVQSAesslQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERAR 423
Cdd:PTZ00121 1585 EAKKAEEARIEE-------VMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  424 QAAEERSHKLQQElsgrgsalqlqlSQLRDQCSGLEKELKSEKEQRQALQRELQREKDtscllqtELQQVEGLKKELREL 503
Cdd:PTZ00121 1654 KAEEENKIKAAEE------------AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKEAEE 1714
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568972939  504 QDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEATHCKQCEKD 565
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
242-523 3.93e-04

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: 43.56  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  242 GLEKTNSKLQEELSAATDRIcslqKEQQQLREQNEVIRERSEKSVEITKqdtKVELETyKQTRQGLDEMYSDVWK----- 316
Cdd:pfam05483 128 ENEKVSLKLEEEIQENKDLI----KENNATRHLCNLLKETCARSAEKTK---KYEYER-EETRQVYMDLNNNIEKmilaf 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  317 ----------------QLKEEKKVRLELEKELELQIGMKtemEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHK 380
Cdd:pfam05483 200 eelrvqaenarlemhfKLKEDHEKIQHLEEEYKKEINDK---EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEK 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  381 VQSAESSLQQKNEA-------IASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRD 453
Cdd:pfam05483 277 TKLQDENLKELIEKkdhltkeLEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA 356
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568972939  454 QCSGLEKELKSEkeqrqalQRELQREKDTSCLLQTELQQVEGLKKELRELQDEK----AELRKVCEEQEQALQE 523
Cdd:pfam05483 357 TTCSLEELLRTE-------QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevelEELKKILAEDEKLLDE 423
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
229-393 4.51e-04

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 43.30  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  229 LSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEiTKQDTKVELETYKQTRQGLD 308
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVS-AKQKDKQTVQQLEKRLKAEQ 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  309 EMYSDVWKQLKEEKKVRLELEKELELQIGM---------------KTEMEIAMKLLEKDTHEKQDTLVALrqqleEVKAI 373
Cdd:pfam09726 479 EARASAEKQLAEEKKRKKEEEATAARAVALaaasrgecteslkqrKRELESEIKKLTHDIKLKEEQIREL-----EIKVQ 553
                         170       180
                  ....*....|....*....|....*..
gi 568972939  374 NLQMFHKVQ-------SAESSLQQKNE 393
Cdd:pfam09726 554 ELRKYKESEkdtevlmSALSAMQDKNQ 580
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
409-512 4.88e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 409 MKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQREL---QREKDTSCL 485
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568972939 486 LQTELQQ----VEGLKKELRELQDEKAELRK 512
Cdd:COG2433  463 KDREISRldreIERLERELEEERERIEELKR 493
PTZ00121 PTZ00121
MAEBL; Provisional
267-556 6.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  267 EQQQLREQNEVIRERSEKSVEITKQDT-KVELETYKQ--TRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEME 343
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETgKAEEARKAEeaKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE 1161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  344 IAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQV--MSSMKQMEERLQQAER 421
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEE 1241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  422 ARQAAEERSHK-LQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQA---LQRELQREKDTSCLLQTELQQVEGLK 497
Cdd:PTZ00121 1242 AKKAEEERNNEeIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeaKKAEEKKKADEAKKKAEEAKKADEAK 1321
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939  498 KELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKghtwLKDDEA 556
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE----KKKEEA 1376
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
238-526 6.51e-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: 43.03  E-value: 6.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   238 TKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIrERSEKSVEITKQDTKVEletykQTRQGLDEMYSDVWKQ 317
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVT-----QIEQQAQRIHTELQSK 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   318 LKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVAL--RQQLEEVKAInLQMFHKVQSAESSLQQKNEAI 395
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsiREISCQQHTL-TQHIHTLQQQKTTLTQKLQSL 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   396 ASfegkttqvmssmKQMEERLQQAERARQAAEERShkLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRE 475
Cdd:TIGR00618  399 CK------------ELDILQREQATIDTRTSAFRD--LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939   476 LQREKDTSCLLQTE---LQQVEGLKKE----LRELQDEKAELRKVCEEQEQALQEMGL 526
Cdd:TIGR00618  465 AQSLKEREQQLQTKeqiHLQETRKKAVvlarLLELQEEPCPLCGSCIHPNPARQDIDN 522
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
363-523 6.55e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 42.75  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 363 LRQQLEEVKAINLQM---------FHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEErshkL 433
Cdd:COG0497  191 LRFQLEELEAAALQPgeeeeleeeRRRLSNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAE----L 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 434 QQELSgrgSAL-QLQ--LSQLRDQCSGLE---KELkSEKEQRQALQRELQR-------------EKdtsclLQTELQQVE 494
Cdd:COG0497  267 AERLE---SALiELEeaASELRRYLDSLEfdpERL-EEVEERLALLRRLARkygvtveellayaEE-----LRAELAELE 337
                        170       180
                 ....*....|....*....|....*....
gi 568972939 495 GLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:COG0497  338 NSDERLEELEAELAEAEAELLEAAEKLSA 366
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
105-155 6.86e-04

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: 41.53  E-value: 6.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 105 VRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKQLLSEFYEPEALM 155
Cdd:cd17690  130 IQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFL 180
PTZ00121 PTZ00121
MAEBL; Provisional
244-564 7.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  244 EKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDtkvELETYKQTRQGLDEMYSDVWKQLKEEKK 323
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD---ELKKAEEKKKADEAKKAEEKKKADEAKK 1309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  324 vrlelekelelqigmKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTT 403
Cdd:PTZ00121 1310 ---------------KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  404 QV---MSSMKQMEERLQQAERARQAAEERSHKlQQELSgRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREK 480
Cdd:PTZ00121 1375 EAkkkADAAKKKAEEKKKADEAKKKAEEDKKK-ADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  481 DTSCLLQTELQQVEGLKKELRELQdEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALKGHTWLKDDEATHCK 560
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531

                  ....
gi 568972939  561 QCEK 564
Cdd:PTZ00121 1532 EAKK 1535
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
414-541 7.37e-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: 42.74  E-value: 7.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   414 ERLQQAErarQAAEERSHKLQQELsgrgSALQLQLSQLRDQCSGLEKEL-------------KSEKEQR-QALQRELQRE 479
Cdd:TIGR02168  242 EELQEEL---KEAEEELEELTAEL----QELEEKLEELRLEVSELEEEIeelqkelyalaneISRLEQQkQILRERLANL 314
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939   480 KDTSCLLQTELQQVEG----LKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEV 541
Cdd:TIGR02168  315 ERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
234-572 7.59e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   234 GDLQTKIDGLEKTNSKLQEELSAA-----TDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDtKVELETYKQTRQGLD 308
Cdd:pfam02463  105 GDSEYYINGKNVTKKEVAELLESQgispeAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLK-RKKKEALKKLIEETE 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   309 EMYSDVWKQLKEEKKVRLelekelelqigmktemeiaMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSL 388
Cdd:pfam02463  184 NLAELIIDLEELKLQELK-------------------LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   389 QQKNEAiasfegKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSA----LQLQLSQLRDQCSGLEKELKS 464
Cdd:pfam02463  245 LLRDEQ------EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKeeeeLKSELLKLERRKVDDEEKLKE 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   465 EKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKA 544
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
                          330       340
                   ....*....|....*....|....*...
gi 568972939   545 LKGHTWLKDDEATHCKQCEKDFSISRRK 572
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKK 426
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
218-540 9.61e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 218 QKNYVEELNRHLScTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEK--SVEITKQDTKV 295
Cdd:PRK02224 201 EKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiaETEREREELAE 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 296 ELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINL 375
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 376 QMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGrgsalqlqlsqLRDQC 455
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE-----------LRERE 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 456 SGLEKELKSEKEQRQALQREL---------QREKDTS--CLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQaLQEM 524
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLeagkcpecgQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEA 507
                        330
                 ....*....|....*.
gi 568972939 525 GLHLSQSKLKMEDIKE 540
Cdd:PRK02224 508 EDRIERLEERREDLEE 523
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
183-477 9.98e-04

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: 42.40  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  183 DLDSQVGVIDFS--LCLKDAQDLDSGREHERI--TDVLDQKNYVEELNRHLSCTVGD--LQTKIDGLEKTNSKLQEElsA 256
Cdd:pfam05483 454 DLEIQLTAIKTSeeHYLKEVEDLKTELEKEKLknIELTAHCDKLLLENKELTQEASDmtLELKKHQEDIINCKKQEE--R 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  257 ATDRICSLQKEQQQLREQNEVIRE-----------RSEKSVEITKQDTKVELETYKQTRQGLD---------EMYSDVWK 316
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREefiqkgdevkcKLDKSEENARSIEYEVLKKEKQMKILENkcnnlkkqiENKNKNIE 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  317 QLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQ-MFHKVQSAESSLQQKNEAI 395
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEkLLEEVEKAKAIADEAVKLQ 691
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  396 ASFEGKTTQVMSSMKQMEERlqQAERARQAAEERSHKL------QQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQR 469
Cdd:pfam05483 692 KEIDKRCQHKIAEMVALMEK--HKHQYDKIIEERDSELglyknkEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769

                  ....*...
gi 568972939  470 QALQRELQ 477
Cdd:pfam05483 770 EKLKMEAK 777
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
222-523 1.00e-03

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: 42.47  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   222 VEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDrICS--------LQKEQQQLREQNEVIRERSEKSVEITKQdt 293
Cdd:pfam01576   17 VKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE-LCAeaeemrarLAARKQELEEILHELESRLEEEEERSQQ-- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   294 kveletYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKElelqigmKTEMEIAMKLLEKDT---HEKQDTLVALRQQLEEv 370
Cdd:pfam01576   94 ------LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLE-------KVTTEAKIKKLEEDIlllEDQNSKLSKERKLLEE- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   371 kainlqmfhKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEershKLQQELSGRGSALQLQLSQ 450
Cdd:pfam01576  160 ---------RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE----KAKRKLEGESTDLQEQIAE 226
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568972939   451 LRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE 299
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
222-522 1.07e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   222 VEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELETYK 301
Cdd:TIGR00618  302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   302 QTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKV 381
Cdd:TIGR00618  382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   382 QSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQEL--SGRGSALQLQLSQLRDQCSGLE 459
Cdd:TIGR00618  462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdIDNPGPLTRRMQRGEQTYAQLE 541
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939   460 KELK-------SEKEQRQALQRELQREKDTSCLLQTELQQV----EGLKKELRELQDE-----KAELRKVCEEQEQALQ 522
Cdd:TIGR00618  542 TSEEdvyhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSkediPNLQNITVRLQDLteklsEAEDMLACEQHALLRK 620
DUF4175 pfam13779
Domain of unknown function (DUF4175);
404-525 1.12e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  404 QVMSSMKQMEERLQQAERARQAAEERShKLQQELSGRGSALQLQlSQLRDQC-SGLEKELKSEKEQRQALQRELQREKDT 482
Cdd:pfam13779 577 QMLSQLQQMLENLQAGQPQQQQQQGQS-EMQQAMDELGDLLREQ-QQLLDETfRQLQQQGGQQQGQPGQQGQQGQGQQPG 654
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568972939  483 SCLLQTELQQV-EGLKKELRELQDEKAELRKVCEEQEQALQEMG 525
Cdd:pfam13779 655 QGGQQPGAQMPpQGGAEALGDLAERQQALRRRLEELQDELKELG 698
zf-RING_5 pfam14634
zinc-RING finger domain;
558-586 1.20e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 37.02  E-value: 1.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 568972939  558 HCKQCEKDFSiSRRKHHCRNCGHIFCNTC 586
Cdd:pfam14634   1 HCNKCFKELS-KTRPFYLTSCGHIFCEEC 28
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
385-523 1.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 385 ESSLQQKNEAIASFEGKTTQVMSsmkqmeERLQQAERARQAAEERSHKLQQelsgrgsaLQLQLSQLRDQCSGLEKELKS 464
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNL------KELKELEEELKEAEEKEEEYAE--------LQEELEELEEELEELEAELEE 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568972939 465 EKEQRQALQRELQREKDTSCLLQTElQQVEGLKKELRELQDEKAELRKVCEEQEQALQE 523
Cdd:COG4717  114 LREELEKLEKLLQLLPLYQELEALE-AELAELPERLEELEERLEELRELEEELEELEAE 171
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
235-402 1.35e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 235 DLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRE-------------RSEKSVEITKQDTKVE----L 297
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlgRQPPLALLLSPEDFLDavrrL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 298 ETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQM 377
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
                        170       180
                 ....*....|....*....|....*
gi 568972939 378 FHKVQSAESSLQQKNEAIASFEGKT 402
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAERT 243
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
234-564 1.60e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   234 GDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKsveITKQDTKVElETYKQTRQGLDEMYSD 313
Cdd:TIGR00618  524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI---LTQCDNRSK-EDIPNLQNITVRLQDL 599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   314 VWKQLKEEKKVRLELEKElelqigmKTEMEIAMKLLEKDTHEKQdtlVALRQQLEEVK----AINLQMFHKVQSAESSLQ 389
Cdd:TIGR00618  600 TEKLSEAEDMLACEQHAL-------LRKLQPEQDLQDVRLHLQQ---CSQELALKLTAlhalQLTLTQERVREHALSIRV 669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   390 QKNEAIASFEGKTT------QVMSSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQlqlsqlrdqcsgleKELK 463
Cdd:TIGR00618  670 LPKELLASRQLALQkmqsekEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG--------------SDLA 735
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   464 SEKEQRQALQRELQREKDTSCLLQTELQQVEGLK-----KELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDi 538
Cdd:TIGR00618  736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS- 814
                          330       340
                   ....*....|....*....|....*.
gi 568972939   539 KEVNKALKGHTWLKDDEATHCKQCEK 564
Cdd:TIGR00618  815 DEDILNLQCETLVQEEEQFLSRLEEK 840
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
315-520 1.63e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 315 WKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKainlQMFHKVQSAESSLQQKNEA 394
Cdd:COG4717  294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ----ELLREAEELEEELQLEELE 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 395 IASFEGKTTQVMSSMKQMEERLQQAERARQAAEER---SHKLQQELSGRGSAL-QLQLSQLRDQCSGLEKELKSEKEQRQ 470
Cdd:COG4717  370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELeelEEQLEELLGELEELLeALDEEELEEELEELEEELEELEEELE 449
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568972939 471 ALQRELQRekdtsclLQTELQQVEGlKKELRELQDEKAELRKVCEEQEQA 520
Cdd:COG4717  450 ELREELAE-------LEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
PRK11637 PRK11637
AmiB activator; Provisional
356-480 1.72e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 356 KQDTLVALRQQLEEVKAinlqmfHKVQSAESSLQQKneaiasfegkttQVMSSMKQMEERLQQAERARQ----AAEERSH 431
Cdd:PRK11637 168 RQETIAELKQTREELAA------QKAELEEKQSQQK------------TLLYEQQAQQQKLEQARNERKktltGLESSLQ 229
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568972939 432 KLQQELsgrgSALQLQLSQLRDQCSGLEKELK--SEKEQRQAlQRELQREK 480
Cdd:PRK11637 230 KDQQQL----SELRANESRLRDSIARAEREAKarAEREAREA-ARVRDKQK 275
Filament pfam00038
Intermediate filament protein;
403-523 1.79e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.67  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  403 TQVMSSMKQMEErlQQAERARQAAEE----RSHKLQQELSGRGSALQ---LQLSQLRDQCSGLEKELKSEKEQRQALQRE 475
Cdd:pfam00038 169 TSALAEIRAQYE--EIAAKNREEAEEwyqsKLEELQQAAARNGDALRsakEEITELRRTIQSLEIELQSLKKQKASLERQ 246
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568972939  476 LQREKDTSCLlqtelqQVEGLKKELRELQDEKAELRkvcEEQEQALQE 523
Cdd:pfam00038 247 LAETEERYEL------QLADYQELISELEAELQETR---QEMARQLRE 285
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
236-471 1.79e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 236 LQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERseksveitKQDTKVELETYKQTRQGLDEMYSdvw 315
Cdd:COG4942   39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------LAELEKEIAELRAELEAQKEELA--- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 316 KQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINlqmfhkvQSAESSLQQKNEAI 395
Cdd:COG4942  108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-------AELEAERAELEALL 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 396 AsfegkttqvmsSMKQMEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQA 471
Cdd:COG4942  181 A-----------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
203-489 1.80e-03

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: 41.64  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   203 LDSGREHER--ITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNS-----------KLQE--ELSAATDRICSLQKE 267
Cdd:pfam15921  470 LESTKEMLRkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAeitklrsrvdlKLQElqHLKNEGDHLRNVQTE 549
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   268 QQQLREQN-------EVIRERSEKSVEITKQDTKVELETYKQTRQgLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKT 340
Cdd:pfam15921  550 CEALKLQMaekdkviEILRQQIENMTQLVGQHGRTAGAMQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   341 EMEI-AMKLLE---------KDTHEKQDTLVA----------------------LRQQLEEVKAINLQMFHKVQSAESSL 388
Cdd:pfam15921  629 DLELeKVKLVNagserlravKDIKQERDQLLNevktsrnelnslsedyevlkrnFRNKSEEMETTTNKLKMQLKSAQSEL 708
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   389 QQKNEAIASFEGKTTQVM---------------------SSMKQMEERLQQAERARQAAEERSHKLQQELS--------- 438
Cdd:pfam15921  709 EQTRNTLKSMEGSDGHAMkvamgmqkqitakrgqidalqSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvateknkm 788
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568972939   439 -GRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTE 489
Cdd:pfam15921  789 aGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
408-546 1.80e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   408 SMKQMEERLQQaERARQaaEERSHKLQQELS---GRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSC 484
Cdd:TIGR02169  685 GLKRELSSLQS-ELRRI--ENRLDELSQELSdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   485 LLQTEL-----------------------QQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEV 541
Cdd:TIGR02169  762 ELEARIeeleedlhkleealndlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                   ....*
gi 568972939   542 NKALK 546
Cdd:TIGR02169  842 RIDLK 846
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
349-523 1.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 349 LEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEE 428
Cdd:COG4372   50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 429 RSHKLQQELSGRGSALQLQLSQLRDqcsgLEKELKSEKEQRQALQRELQREKDtscllQTELQQVEGLKKELRELQDEKA 508
Cdd:COG4372  130 QRKQLEAQIAELQSEIAEREEELKE----LEEQLESLQEELAALEQELQALSE-----AEAEQALDELLKEANRNAEKEE 200
                        170
                 ....*....|....*
gi 568972939 509 ELRKVCEEQEQALQE 523
Cdd:COG4372  201 ELAEAEKLIESLPRE 215
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
366-540 1.93e-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: 41.36  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   366 QLEEVKAINLQMFHKVQSAESSLQQKNEAiasfegkTTQVMSSMKqmeERLQQAERARQAAEERSHKLQQELSGRGSALQ 445
Cdd:pfam12128  277 RQEERQETSAELNQLLRTLDDQWKEKRDE-------LNGELSAAD---AAVAKDRSELEALEDQHGAFLDADIETAAADQ 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   446 LQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKdtSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQAL-QEM 524
Cdd:pfam12128  347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR--SKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSEL 424
                          170
                   ....*....|....*.
gi 568972939   525 GLHLSQSKLKMEDIKE 540
Cdd:pfam12128  425 REQLEAGKLEFNEEEY 440
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
275-543 2.22e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   275 NEVIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIG--MKTEMEIAMKLLEKD 352
Cdd:pfam02463  625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESelAKEEILRRQLEIKKK 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   353 THEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIAsfegkttqvmssmkqMEERLQQAERARQAAEERSHK 432
Cdd:pfam02463  705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE---------------EEEEEKSRLKKEEKEEEKSEL 769
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   433 LQQELSGRGSA----LQLQLSQLRDQCSGLEKELKSEKEQRQ---ALQRELQREKDTSCLLQTELQQVEGLKKELRELQD 505
Cdd:pfam02463  770 SLKEKELAEERekteKLKVEEEKEEKLKAQEEELRALEEELKeeaELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 568972939   506 EKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNK 543
Cdd:pfam02463  850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
Gp58 pfam07902
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ...
278-456 2.61e-03

gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.


Pssm-ID: 369586 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  278 IRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQL--KEEKKVRLELEKELELQIGMKTEMEIAM--------- 346
Cdd:pfam07902 126 IVESAEGIATRISEDTDKKLALINETISGIRREYQDADRQLssSYQAGIEGLKATMASDKIGLQAEIQASAqglsqrydn 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  347 ---KLLEKDTHEKQDTLVALRQQLEEVKA----INLQMFHKVQSAESSLQ--------QKNEAIASFEGKTTQVMSSMKQ 411
Cdd:pfam07902 206 eirKLSAKITTTSSGTTEAYESKLDDLRAeftrSNQGMRTELESKISGLQstqqstayQISQEISNREGAVSRVQQDLDS 285
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568972939  412 MEERLQQAERARQAAEERSHKLQQELSGRGSALQLQLSQLRDQCS 456
Cdd:pfam07902 286 YQRRLQDAEKNYSSLTQTVKGLQSTVSDPNSKLESRITQLAGLIE 330
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
198-561 2.76e-03

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: 40.93  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   198 KDAQDLDSGREHEritDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEV 277
Cdd:pfam01576  634 KETRALSLARALE---EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   278 IrERSEKSVEITKQDTKVELETYKQTRQGL-DEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDThek 356
Cdd:pfam01576  711 T-EDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQI--- 786
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   357 QDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASF---EGKTTQVMSSMKQMEERLQQAERARQAAEERSHKL 433
Cdd:pfam01576  787 DAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSkesEKKLKNLEAELLQLQEDLAASERARRQAQQERDEL 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   434 QQELSGRG---SALQLQLSQLRDQCSGLEKELKSEK--------------EQRQALQRELQREKDTSCLLQTELQQVEGL 496
Cdd:pfam01576  867 ADEIASGAsgkSALQDEKRRLEARIAQLEEELEEEQsntellndrlrkstLQVEQLTTELAAERSTSQKSESARQQLERQ 946
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939   497 KKELR-ELQDEKAELR------------KVCEEQEQALQEMGLHLSQSKLkmedIKEVNKALKGHTWLKDDEATHCKQ 561
Cdd:pfam01576  947 NKELKaKLQEMEGTVKskfkssiaaleaKIAQLEEQLEQESRERQAANKL----VRRTEKKLKEVLLQVEDERRHADQ 1020
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
219-553 2.90e-03

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: 40.87  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   219 KNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITK---QDTKV 295
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRnqlQNTVH 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   296 ELETYKQTRQgldEMYSDVWKQLKEEKKVrlelekelelqigmktemeiaMKLLEKDTHEKQDTLVALRQ----QLEEVK 371
Cdd:pfam15921  153 ELEAAKCLKE---DMLEDSNTQIEQLRKM---------------------MLSHEGVLQEIRSILVDFEEasgkKIYEHD 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   372 AINLQMFHKVQSAESS-LQQKNEAIASFEGKTTQVMSSMKQMEERLQ-QAERARQAAEERSHKLQQELSGRGSALQLQLS 449
Cdd:pfam15921  209 SMSTMHFRSLGSAISKiLRELDTEISYLKGRIFPVEDQLEALKSESQnKIELLLQQHQDRIEQLISEHEVEITGLTEKAS 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   450 QLRDQCSGLEKELKSEKEQRQ----ALQRELQREKDTSCLLQTELQQ--------VEGLKKELRELQDEKAELRKvceEQ 517
Cdd:pfam15921  289 SARSQANSIQSQLEIIQEQARnqnsMYMRQLSDLESTVSQLRSELREakrmyedkIEELEKQLVLANSELTEART---ER 365
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 568972939   518 EQALQEMG------------LHLSQSKLKMEdiKEVNKALkghtWLKD 553
Cdd:pfam15921  366 DQFSQESGnlddqlqklladLHKREKELSLE--KEQNKRL----WDRD 407
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
393-546 2.95e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 393 EAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQELsgrgSALQLQLSQLRDQCSGLEKELKSEKEQRQAL 472
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQA 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568972939 473 QRELQREKDTSCLLQTELQQVEG----LKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKMEDIKEVNKALK 546
Cdd:COG4372  100 QEELESLQEEAEELQEELEELQKerqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
mukB PRK04863
chromosome partition protein MukB;
234-530 3.13e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  234 GDLQTKIDGLEKTNSKLQEELSAATDR-----------------ICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVE 296
Cdd:PRK04863  310 VEMARELAELNEAESDLEQDYQAASDHlnlvqtalrqqekieryQADLEELEERLEEQNEVVEEADEQQEENEARAEAAE 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  297 LEtYKQTRQGLdemySDVWKQLKEEKKvrlelekelelqigMKTEMEIAMKLLEK----------DTHEKQDTLVALRQQ 366
Cdd:PRK04863  390 EE-VDELKSQL----ADYQQALDVQQT--------------RAIQYQQAVQALERakqlcglpdlTADNAEDWLEEFQAK 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  367 LEEVKAINLQMFHKVQSAESSLQQKNEAIASFE-----------------------------GKTTQVMSSMKQMEERLQ 417
Cdd:PRK04863  451 EQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagevsrseawdvarellrrlreqrhlaEQLQQLRMRLSELEQRLR 530
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  418 Q---AERARQAAEERSHK----------LQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQ----------ALQR 474
Cdd:PRK04863  531 QqqrAERLLAEFCKRLGKnlddedeleqLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQrlaarapawlAAQD 610
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  475 ELQREKDTSCLLQTELQQVEGLKKEL----RELQDEKAELrkvcEEQEQALQEMGLHLSQ 530
Cdd:PRK04863  611 ALARLREQSGEEFEDSQDVTEYMQQLlereRELTVERDEL----AARKQALDEEIERLSQ 666
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-524 3.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 238 TKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELETyKQTRQGLDEMYSDVwKQ 317
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL-PELREELEKLEKEV-KE 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 318 LKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKainlqmfhkvqsaesSLQQKNEAIAS 397
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------------ELKEKAEEYIK 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 398 FEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLqQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQ 477
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568972939 478 REKDTSCL----LQTELQQVEGLKKELRE----LQDEKAELRKVCEEQEQALQEM 524
Cdd:PRK03918 377 LKKRLTGLtpekLEKELEELEKAKEEIEEeiskITARIGELKKEIKELKKAIEEL 431
PRK09039 PRK09039
peptidoglycan -binding protein;
433-521 3.70e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 433 LQQELSGRGSALQ---LQLSQLRDQcsglekeLKSEKEQRQALQRELQRekdtsclLQTELQQVEGLKKELRELQDEKAE 509
Cdd:PRK09039  44 LSREISGKDSALDrlnSQIAELADL-------LSLERQGNQDLQDSVAN-------LRASLSAAEAERSRLQALLAELAG 109
                         90
                 ....*....|..
gi 568972939 510 LRKVCEEQEQAL 521
Cdd:PRK09039 110 AGAAAEGRAGEL 121
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
243-528 3.94e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.11  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  243 LEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELETYK------QTRQGLDEMYSDVWK 316
Cdd:pfam05557  32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKklnekeSQLADAREVISCLKN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  317 QLKEEKkvrlelekelelQIGMKTEMEiamklLEKDTHEKQDtlvaLRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIA 396
Cdd:pfam05557 112 ELSELR------------RQIQRAELE-----LQSTNSELEE----LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  397 sfegkttqvmsSMKQMEERLQQAERARQAAEershKLQQELsGRGSALQLQLSQLRDQcsglEKELKSEKEQRQALQREL 476
Cdd:pfam05557 171 -----------RIKELEFEIQSQEQDSEIVK----NSKSEL-ARIPELEKELERLREH----NKHLNENIENKLLLKEEV 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568972939  477 QRekdtsclLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHL 528
Cdd:pfam05557 231 ED-------LKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNL 275
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
210-524 4.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 210 ERITDVLDQKNYVEELNRHL--SCTVGDLQtkIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSE---- 283
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLlaEAGLDDAD--AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADdlee 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 284 ---------KSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTH 354
Cdd:PRK02224 357 raeelreeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 355 EKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAA------EE 428
Cdd:PRK02224 437 TARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierlEE 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 429 RSHKLQQELSGRGSAL---QLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKDTSCLLQTELQQV----EGLKKeLR 501
Cdd:PRK02224 517 RREDLEELIAERRETIeekRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkeriESLER-IR 595
                        330       340
                 ....*....|....*....|....*.
gi 568972939 502 ELQDEKAELRKVCE---EQEQALQEM 524
Cdd:PRK02224 596 TLLAAIADAEDEIErlrEKREALAEL 621
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
338-507 4.83e-03

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: 40.12  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  338 MKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVkainlqmfhkVQSAESSLQQKNEAIASfegkttqvmssmkqMEERLQ 417
Cdd:pfam07111 493 LDAELQLSAHLIQQEVGRAREQGEAERQQLSEV----------AQQLEQELQRAQESLAS--------------VGQQLE 548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  418 QAERARQAAEERSHKLQQELSGR----GSALQLQLSQ----LRDQCSGLEKEL-KSEKEQRQA------LQRELQREKDT 482
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELTQQqeiyGQALQEKVAEvetrLREQLSDTKRRLnEARREQAKAvvslrqIQHRATQEKER 628
                         170       180       190
                  ....*....|....*....|....*....|
gi 568972939  483 SC---LLQTELQQVEG--LKKELRELQDEK 507
Cdd:pfam07111 629 NQelrRLQDEARKEEGqrLARRVQELERDK 658
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
352-523 4.84e-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: 40.21  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   352 DTHEKQDTLVALRQQLEEvkaiNLQMFH-KVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEErs 430
Cdd:pfam12128  594 EWAASEEELRERLDKAEE----ALQSAReKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKD-- 667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   431 hKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRELQREKdtscllQTELQQVEG-LKKELRELQDEKAE 509
Cdd:pfam12128  668 -KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK------QAYWQVVEGaLDAQLALLKAAIAA 740
                          170
                   ....*....|....
gi 568972939   510 LRKVCEEQEQALQE 523
Cdd:pfam12128  741 RRSGAKAELKALET 754
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
558-590 4.93e-03

RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438405  Cd Length: 37  Bit Score: 35.08  E-value: 4.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568972939 558 HCKQCEK----DFSISrrkhhcrNCGHIFCNTCSSNE 590
Cdd:cd16747    2 HCNKCFRrdgaSFFIT-------SCGHIFCEKCIKAE 31
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
260-518 5.60e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  260 RICSLQKEQQQLREQNEVIRERSEKS--VEITKQDTKVELETYKQTRQGLDEMysdvwkQLKEEKkvrlelekelelqig 337
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNENIENKllLKEEVEDLKRKLEREEKYREEAATL------ELEKEK--------------- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  338 MKTEMEiAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQME---- 413
Cdd:pfam05557 257 LEQELQ-SWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNkklk 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  414 ------ERLQQ------AER-----------ARQAAEERSHKLQQELSGRGSALQ---LQLSQLRDQCSGLEKELKSEKE 467
Cdd:pfam05557 336 rhkalvRRLQRrvllltKERdgyrailesydKELTMSNYSPQLLERIEEAEDMTQkmqAHNEEMEAQLSVAEEELGGYKQ 415
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568972939  468 QRQALQRELQREKDTSCLLQ--TELQQVEGLKKELRELQDEKAELRKVCEEQE 518
Cdd:pfam05557 416 QAQTLERELQALRQQESLADpsYSKEEVDSLRRKLETLELERQRLREQKNELE 468
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
219-538 5.69e-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: 39.81  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  219 KNYVEELNRHLS---CTVGDLQTKIDGLEKTNSK-------LQEELSAATDRICSLQKEQQQLR----EQNEVIRERSEK 284
Cdd:pfam10174 288 KNKIDQLKQELSkkeSELLALQTKLETLTNQNSDckqhievLKESLTAKEQRAAILQTEVDALRlrleEKESFLNKKTKQ 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  285 SVEITKQ---------DTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHE 355
Cdd:pfam10174 368 LQDLTEEkstlageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSE 447
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  356 KQDTLVALRQQ-----------LEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQ 424
Cdd:pfam10174 448 KERIIERLKEQreredrerleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  425 AAEERSHKLQ-QELSGRGSALQLQLS-QLRDQCSGLEKELKSEKEQRQALQRELQR---------------EKDTSCLLQ 487
Cdd:pfam10174 528 QKKEECSKLEnQLKKAHNAEEAVRTNpEINDRIRLLEQEVARYKEESGKAQAEVERllgilrevenekndkDKKIAELES 607
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568972939  488 TELQQVEGLKKELRELQDEKAELRK--VCEEQEQALQEMGLHLSQSKLKMEDI 538
Cdd:pfam10174 608 LTLRQMKEQNKKVANIKHGQQEMKKkgAQLLEEARRREDNLADNSQQLQLEEL 660
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
355-465 5.74e-03

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: 39.94  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  355 EKQDTLVALRQQLEEVKAINLQM------FHKVQSAESSLQ-QKNEAIASfegkTTQVMSSMKQMEERLQQAERARQAAE 427
Cdd:COG3096   575 EAVEQRSELRQQLEQLRARIKELaarapaWLAAQDALERLReQSGEALAD----SQEVTAAMQQLLEREREATVERDELA 650
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568972939  428 ERSHKLQQE---LSGRGSALQLQLSQLRDQCSGlekELKSE 465
Cdd:COG3096   651 ARKQALESQierLSQPGGAEDPRLLALAERLGG---VLLSE 688
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
392-525 6.49e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939 392 NEAIASFEgkttqvmSSMKQMEERLQQAERARQAAEershKLQQELsgrgsalQLQLSQLRDQcsglEKELKSEKEQ--R 469
Cdd:PRK00409 519 NELIASLE-------ELERELEQKAEEAEALLKEAE----KLKEEL-------EEKKEKLQEE----EDKLLEEAEKeaQ 576
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939 470 QALqRELQREKDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMG 525
Cdd:PRK00409 577 QAI-KEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQK 631
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
236-536 7.16e-03

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: 39.35  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  236 LQTKIDGLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKVELEtykqtrQGLDEMYSDVW 315
Cdd:pfam07111 167 LTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE------QVPPEVHSQTW 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  316 KQLKEEkkvrlelekelelqigmktemeiamkLLEKDTHEKQDTlVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAI 395
Cdd:pfam07111 241 ELERQE--------------------------LLDTMQHLQEDR-ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPS 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  396 ASFEGKTTQVMSSMkqmeerlqqaeraRQAAEERSHKLQQELSGRGSALQLQLSQLRDQCSGLEKELKSEKEQRQALQRE 475
Cdd:pfam07111 294 DSLEPEFPKKCRSL-------------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRA 360
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568972939  476 LQrekDTSCLLQTELQQVEGLKKELRELQDEKAELRKVCEEQEQALQEMGLHLSQSKLKME 536
Cdd:pfam07111 361 LQ---DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
235-540 8.24e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.26  E-value: 8.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   235 DLQTKIDgLEKTNSKLQEELSAATDRICSLQKEQQQLREQNEVIRERSEKSVEITKQDTKvELETYKQTRQGLD----EM 310
Cdd:TIGR00606  686 VFQTEAE-LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK-EIPELRNKLQKVNrdiqRL 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   311 YSDVWKQLKEEKKVRLELEKELELQIGM-----------KTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFH 379
Cdd:TIGR00606  764 KNDIEEQETLLGTIMPEEESAKVCLTDVtimerfqmelkDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   380 KVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQAERARQAAEERSHKLQQelsgrgsaLQLQLSQLRDQCSGLE 459
Cdd:TIGR00606  844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS--------LIREIKDAKEQDSPLE 915
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939   460 KELKSEKEQRQAL----QRELQREKDTSCLLQTELQQVEGLKKEL-RELQDEKAELRKvceEQEQALQEMGLHLSQSKLK 534
Cdd:TIGR00606  916 TFLEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIeNKIQDGKDDYLK---QKETELNTVNAQLEECEKH 992

                   ....*.
gi 568972939   535 MEDIKE 540
Cdd:TIGR00606  993 QEKINE 998
mukB PRK04863
chromosome partition protein MukB;
345-498 8.40e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972939  345 AMKLLEKDthekQDTLVALRQQLEEVKAINLQMFHKVQSAESSLQQKNEAIASFEGKTTQVMSSMKQMEERLQQ-AERAR 423
Cdd:PRK04863  976 AAEMLAKN----SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlGVPAD 1051
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568972939  424 QAAEERSHKLQQELSGRgsalqlqLSQLRDQCSGLEKELKSEKEQRQALQRELQR-EKDtsclLQTELQQVEGLKK 498
Cdd:PRK04863 1052 SGAEERARARRDELHAR-------LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKlERD----YHEMREQVVNAKA 1116
 
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