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Conserved domains on  [gi|578835464|ref|XP_006723651|]
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kinesin-like protein KIF16B isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 578835464  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.43e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 578835464  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1178-1281 1.24e-59

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


:

Pssm-ID: 132784  Cd Length: 127  Bit Score: 200.30  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1178 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQSATSPLHiNK 1257
Cdd:cd06874    25 ITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQLETYLRNFFSVCLKLPACPLY-PK 103

                          90       100
                  ....*....|....*....|....
gi 578835464 1258 VGLTLSKHTICEFSPFFKKGVFDY 1281
Cdd:cd06874   104 VGRTLSKATLCDFSPFFRKGVFEN 127
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 606-1089 1.02e-15

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.68  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  606 RLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196   303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196   383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  765 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  843 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 912
Cdd:COG1196   538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 992
Cdd:COG1196   613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1072
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                         490
                  ....*....|....*..
gi 578835464 1073 KDQERLEYEIQQLKQKI 1089
Cdd:COG1196   760 PDLEELERELERLEREI 776
Kinesin_assoc super family cl24686
Kinesin-associated;
364-476 3.39e-11

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.32  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 578835464   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 578835464  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 3-365 3.93e-151

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 458.57  E-value: 3.93e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 578835464    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 8.18e-150

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 454.72  E-value: 8.18e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578835464   327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 9.59e-80

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 273.92  E-value: 9.59e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  406 EKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059   394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 578835464  477 QT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059   474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.43e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 578835464  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-392 8.66e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 269.88  E-value: 8.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454

                         410       420
                  ....*....|....*....|
gi 578835464  373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1178-1281 1.24e-59

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 200.30  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1178 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQSATSPLHiNK 1257
Cdd:cd06874    25 ITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQLETYLRNFFSVCLKLPACPLY-PK 103

                          90       100
                  ....*....|....*....|....
gi 578835464 1258 VGLTLSKHTICEFSPFFKKGVFDY 1281
Cdd:cd06874   104 VGRTLSKATLCDFSPFFRKGVFEN 127
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 606-1089 1.02e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.68  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  606 RLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196   303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196   383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  765 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  843 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 912
Cdd:COG1196   538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 992
Cdd:COG1196   613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1072
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                         490
                  ....*....|....*..
gi 578835464 1073 KDQERLEYEIQQLKQKI 1089
Cdd:COG1196   760 PDLEELERELERLEREI 776
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 624-937 1.88e-12

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: 71.69  E-value: 1.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLREQQEIEL 703
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERIRQ 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   704 QKKRQEEETfLRVQE---ELQRLKELnnnekaekfqifqELDQLQKEKDEQYAKLELEKKR----LEEQEKEQVMLVAHL 776
Cdd:pfam17380  356 EERKRELER-IRQEEiamEISRMREL-------------ERLQMERQQKNERVRQELEAARkvkiLEEERQRKIQQQKVE 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   777 EEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQlvklvnlEKDLV 855
Cdd:pfam17380  422 MEQIRAEQEEA---RQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR-------KRAEE 491

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   856 QQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEK 935
Cdd:pfam17380  492 QRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565


                   ..
gi 578835464   936 QR 937
Cdd:pfam17380  566 SR 567
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 1182-1239 6.01e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 62.64  E-value: 6.01e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464  1182 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1239
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQ 63
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 1160-1239 1.22e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 62.36  E-value: 1.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   1160 KDNEKLHNGTIqrklkYEITVLD--ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVIAERRSHL 1234
Cdd:smart00312    6 KIGDGKHYYYV-----IEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGL 80


                    ....*
gi 578835464   1235 EKYLR 1239
Cdd:smart00312   81 EKYLQ 85
PTZ00121 PTZ00121
MAEBL; Provisional
 610-870 1.27e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  682 dLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQyaKLELEKKR 761
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKK 1676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  762 LEEQEKEQVMLVAHLEEQLREKQEM--IQLLRRGEvqwvEEEKRDLEGIR----ESLLRVKEARAGGDEDGEELEKAQLR 835
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKE----AEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578835464  836 FFEFKRRQLVKLVNLEKDLVQQKD---ILKKEVQEEQE 870
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEkeaVIEEELDEEDE 1790
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 3.39e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.32  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 578835464   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-905 3.55e-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: 3.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLA 685
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   686 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   766 EKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLV 845
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   846 KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 905
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.38e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                  ...
gi 578835464  549 FRF 551
Cdd:COG1716    91 LRF 93
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 471-555 1.20e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 44.94  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 578835464   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 618-818 7.38e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269    87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHL 776
Cdd:cd16269   155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578835464  777 EEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269   229 EDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 578835464  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 3-365 3.93e-151

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 458.57  E-value: 3.93e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 578835464    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 8.18e-150

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 454.72  E-value: 8.18e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578835464   327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 3-356 1.08e-140

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 430.52  E-value: 1.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106    66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106   145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106   223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 578835464  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106   292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 3-358 5.84e-118

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 370.64  E-value: 5.84e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371   148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371   226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 578835464  318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371   294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 3-358 7.77e-115

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 362.42  E-value: 7.77e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372    62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372   140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372   220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 578835464  309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372   291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 3-358 5.37e-104

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 333.16  E-value: 5.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370    76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370   154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370   231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 578835464  315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370   302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 4-367 7.75e-102

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 327.54  E-value: 7.75e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373    64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373   144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373   221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578835464  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373   293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 3-358 1.77e-101

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 325.44  E-value: 1.77e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374   138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374   215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 578835464  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374   285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 9-360 1.19e-98

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 318.00  E-value: 1.19e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366    71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366   148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366   225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 578835464  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366   288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 1-358 1.45e-98

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 317.73  E-value: 1.45e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYSADTkspdyvsQEMVF 79
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFDPNTT-------QEDVY 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369    62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369   140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369   215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 578835464  317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369   284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 1-367 1.07e-87

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 288.84  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364   145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364   225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835464  305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364   291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 9.59e-80

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 273.92  E-value: 9.59e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  406 EKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059   394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 578835464  477 QT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059   474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.43e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 578835464  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-392 8.66e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 269.88  E-value: 8.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454

                         410       420
                  ....*....|....*....|
gi 578835464  373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 4-356 1.07e-72

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 246.15  E-value: 1.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368    78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368   150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368   230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 578835464  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368   303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 3-356 5.37e-71

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 240.95  E-value: 5.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375     1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375    68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375   145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375   225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 578835464  316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375   294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 4-356 9.24e-68

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 231.24  E-value: 9.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376    66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376   142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376   219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285

                         330       340       350
                  ....*....|....*....|....*....|....
gi 578835464  323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376   286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 4-356 3.69e-67

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 229.88  E-value: 3.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367    63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367   141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367   217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 578835464  309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367   280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 446-554 3.41e-65

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 215.60  E-value: 3.41e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708     1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80

                          90       100
                  ....*....|....*....|....*....
gi 578835464  526 GVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708    81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1178-1281 1.24e-59

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 200.30  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1178 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQSATSPLHiNK 1257
Cdd:cd06874    25 ITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQLETYLRNFFSVCLKLPACPLY-PK 103

                          90       100
                  ....*....|....*....|....
gi 578835464 1258 VGLTLSKHTICEFSPFFKKGVFDY 1281
Cdd:cd06874   104 VGRTLSKATLCDFSPFFRKGVFEN 127
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 446-564 4.49e-49

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 169.96  E-value: 4.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578835464  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 438-561 1.70e-34

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 128.21  E-value: 1.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713     1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 578835464  518 sGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713    78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 453-553 6.42e-32

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 120.03  E-value: 6.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80

                          90       100
                  ....*....|....*....|.
gi 578835464  533 THLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 450-554 7.42e-27

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 105.81  E-value: 7.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707     4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83

                          90       100
                  ....*....|....*....|....*
gi 578835464  530 VEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707    84 SEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 454-562 1.07e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 103.08  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578835464  529 IVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 454-554 2.38e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 101.52  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80

                          90       100
                  ....*....|....*....|..
gi 578835464  533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709    81 TELHHLDRVILGSNHLYVFVGP 102
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 454-556 3.58e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 101.27  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82

                          90       100
                  ....*....|....*....|....*...
gi 578835464  529 IVEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 6-288 9.59e-24

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 99.34  E-value: 9.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363     1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363    42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363   100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578835464  243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363   137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 1178-1275 6.01e-23

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 95.11  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1178 ITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQsaTSPlhinK 1257
Cdd:cd07277    25 IRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRVVNTLIQ--TSP----E 98

                          90
                  ....*....|....*...
gi 578835464 1258 VGLTLSKHTICEFSPFFK 1275
Cdd:cd07277    99 LTACPSKETLIKLLPFFG 116
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 471-554 1.60e-20

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 87.73  E-value: 1.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706    19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97


                  ....
gi 578835464  551 FNHP 554
Cdd:cd22706    98 LNCP 101
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 454-553 2.20e-18

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 81.46  E-value: 2.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77

                          90       100
                  ....*....|....*....|....*
gi 578835464  529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 1164-1243 9.93e-16

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 74.32  E-value: 9.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1164 KLHNGTIQRKLKYEITV---LDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1240
Cdd:cd06093     8 EKVKDGGKKYVVYIIEVttqGGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQLEQYLQS 87


                  ...
gi 578835464 1241 FFS 1243
Cdd:cd06093    88 LLN 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 606-1089 1.02e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.68  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  606 RLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196   303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196   383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  765 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  843 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 912
Cdd:COG1196   538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 992
Cdd:COG1196   613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1072
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                         490
                  ....*....|....*..
gi 578835464 1073 KDQERLEYEIQQLKQKI 1089
Cdd:COG1196   760 PDLEELERELERLEREI 776
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 453-554 5.69e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 71.97  E-value: 5.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711     1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 578835464  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 611-1088 9.99e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.60  E-value: 9.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 688
Cdd:COG1196   216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  689 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 768
Cdd:COG1196   291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  769 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 847
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  848 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 927
Cdd:COG1196   431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  928 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:COG1196   511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  999 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASL 1064
Cdd:COG1196   591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670

                         490       500
                  ....*....|....*....|....
gi 578835464 1065 EAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELE 694
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 3-162 1.05e-14

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 72.64  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464     3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464    83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796   77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 456-564 1.11e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 65.68  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729     4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 578835464  535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 1176-1238 1.86e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 65.37  E-value: 1.86e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1176 YEITVL-------DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYL 1238
Cdd:cd06873    25 YAISVTriypngqEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYL 94
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 624-937 1.88e-12

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: 71.69  E-value: 1.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLREQQEIEL 703
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERIRQ 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   704 QKKRQEEETfLRVQE---ELQRLKELnnnekaekfqifqELDQLQKEKDEQYAKLELEKKR----LEEQEKEQVMLVAHL 776
Cdd:pfam17380  356 EERKRELER-IRQEEiamEISRMREL-------------ERLQMERQQKNERVRQELEAARkvkiLEEERQRKIQQQKVE 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   777 EEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQlvklvnlEKDLV 855
Cdd:pfam17380  422 MEQIRAEQEEA---RQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR-------KRAEE 491

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   856 QQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEK 935
Cdd:pfam17380  492 QRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565


                   ..
gi 578835464   936 QR 937
Cdd:pfam17380  566 SR 567
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 1182-1239 6.01e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 62.64  E-value: 6.01e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464  1182 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1239
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQ 63
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 1160-1239 1.22e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 62.36  E-value: 1.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   1160 KDNEKLHNGTIqrklkYEITVLD--ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVIAERRSHL 1234
Cdd:smart00312    6 KIGDGKHYYYV-----IEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGL 80


                    ....*
gi 578835464   1235 EKYLR 1239
Cdd:smart00312   81 EKYLQ 85
PTZ00121 PTZ00121
MAEBL; Provisional
 610-870 1.27e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  682 dLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQyaKLELEKKR 761
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKK 1676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  762 LEEQEKEQVMLVAHLEEQLREKQEM--IQLLRRGEvqwvEEEKRDLEGIR----ESLLRVKEARAGGDEDGEELEKAQLR 835
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKE----AEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578835464  836 FFEFKRRQLVKLVNLEKDLVQQKD---ILKKEVQEEQE 870
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEkeaVIEEELDEEDE 1790
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 1177-1238 1.52e-11

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 62.68  E-value: 1.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835464 1177 EITVLDETWTVFRRYSRFREMHKTLKLKYAELAALeFPPKKLFGNKDERVIAERRSHLEKYL 1238
Cdd:cd06875    23 EVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDL-LPPKKLIGNKSPSFVEKRRKELEIYL 83
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 1182-1238 2.54e-11

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 61.99  E-value: 2.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1182 DETWTVFRRYSRFREMHKTLKLKYAELAaleFPPKKLFGNKDERVIAERRSHLEKYL 1238
Cdd:cd06871    35 ENSWQVIRRYNDFDLLNASLQISGISLP---LPPKKLIGNMDREFIAERQQGLQNYL 88
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 3.39e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.32  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 578835464   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-905 3.55e-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: 3.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLA 685
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   686 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   766 EKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLV 845
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   846 KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 905
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 456-554 4.80e-11

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 60.70  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79

                          90       100
                  ....*....|....*....|
gi 578835464  535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 611-919 6.18e-11

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: 67.07  E-value: 6.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   611 RQQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQE-ESLKRRSFHIE-NKLK 681
Cdd:pfam17380  302 RQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAMERE---RELERIRQEERKRElERIRQEEIAMEiSRMR 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   682 DLlaEKEKFEEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQE-LDQLQKEKDEQYAKLELEKK 760
Cdd:pfam17380  379 EL--ERLQMERQQKNERVRQELEAARKV-----KILEEERQRKIQQQKVEMEQIRAEQEeARQREVRRLEEERAREMERV 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   761 RLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR-----DLEGIRESLLRVKEARAGGDEDGEELEKAQlr 835
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERKRKLLEKEMEERQKAI-- 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   836 FFEFKRRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKESRLLEkhDESVTDVTEVPQDFEKIKPVeYRL 913
Cdd:pfam17380  530 YEEERRREAEEERRKQQEMEERRRIQEqmRKATEERSRLEAMEREREMMRQIVE--SEKARAEYEATTPITTIKPI-YRP 606


                   ....*.
gi 578835464   914 QYKERQ 919
Cdd:pfam17380  607 RISEYQ 612
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 610-1030 9.27e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  690 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1196   419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQ---WVEEEKRDLEGIRESLLRVKEARAggDEDGEELEKAQLRFFEFKRRQL 844
Cdd:COG1196   499 AEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATF 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVP-QDFEKIKPVEYRLQYKERQLQYL 923
Cdd:COG1196   577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGG 656

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  924 LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKE 1003
Cdd:COG1196   657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 578835464 1004 ILESREKQQ----------------REALERALARLERRHSAL 1030
Cdd:COG1196   737 LLEELLEEEelleeealeelpeppdLEELERELERLEREIEAL 779
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 613-944 2.54e-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: 65.09  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   613 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 692
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   693 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 767
Cdd:TIGR02169  738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   768 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 833
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977

                          330       340       350
                   ....*....|....*....|....*....|....
gi 578835464   914 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 944
Cdd:TIGR02169  978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 455-551 9.13e-10

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 56.51  E-value: 9.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060     1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74

                          90
                  ....*....|....*...
gi 578835464  534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060    75 PLQDGDVIRLGDTT-FRF 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 612-872 1.69e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   612 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaEK 687
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ---YAKLELEKKRLEE 764
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   765 QEKEQVMLVAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRFFEFK- 840
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELS-EELRELESKr 910

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 578835464   841 ---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:TIGR02168  911 selRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 614-1147 1.74e-09

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: 62.39  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   614 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 690
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   691 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 767
Cdd:TIGR02169  440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEK---------RDLEGIRESLLRVKEARAGG 822
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAvakeaiellKRRKAGRATFLPLNKMRDER 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   823 DEDGEELEKAQLRF---------------------------FEFKRRQL--VKLVNLEKDLVQQ---------------- 857
Cdd:TIGR02169  588 RDLSILSEDGVIGFavdlvefdpkyepafkyvfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggil 667

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   858 -KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTdvtEVPQDFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLEE 934
Cdd:TIGR02169  668 fSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEIEQLEQEEekLKERLEE 741

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   935 KQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEIL 1005
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  1006 ESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQ 1084
Cdd:TIGR02169  822 NRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835464  1085 LKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1147
Cdd:TIGR02169  901 LERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
PTZ00121 PTZ00121
MAEBL; Provisional
 555-824 1.98e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  555 KEAAKLREKRKSGLLSSFSLSMTDLSKSREN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  633 KQKSDKAELERMQQEVEtqrkETEIVQLQIRKQEESLKRrsfhienKLKDLLAEKEKfeeerlreqqeielqkKRQEEET 712
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKK-------KAEEAKKAEED----------------EKKAAEA 1693

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  713 FLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLRR 792
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEK----KKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKE 1765

                         250       260       270
                  ....*....|....*....|....*....|..
gi 578835464  793 GEVQWVEEEKRDLEGIRESLLRVKEARAGGDE 824
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 611-1089 2.05e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 690
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   691 EEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEK-DEQYAKLELEKKRLEEQEKEQ 769
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERL 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   770 VMLVAHLEEQLREKQEMIQLLRRGEVQwveeekrdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRqLVKLVN 849
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELIS 530

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   850 LEK------DLVQQKDILKKEVQEEQEILECLkcEHDKESRL---------LEKHDESVTDVTEVPQDFEKIKPVEYRLQ 914
Cdd:TIGR02168  531 VDEgyeaaiEAALGGRLQAVVVENLNAAKKAI--AFLKQNELgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLV 608

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   915 YKERQLQYLLQNHLPTLL--EEKQRAFEILDR-----------------------GPLSLDNTLYQVEKEMEEKEEQLAQ 969
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEE 688

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   970 YQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLAS 1049
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEE 765

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 578835464  1050 LNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1089
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 1153-1239 5.41e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 55.03  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1153 STSADTMKDNEKLHngtiqrkLKYEITV-----LDETWTVF-RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDER 1225
Cdd:cd07279     5 IVSARTVKEGEKKY-------VVYQLAVvqtgdPDTQPAFIeRRYSDFLKLYKALRKQHpQLMAKVSFPRKVLMGNFSSE 77

                          90
                  ....*....|....
gi 578835464 1226 VIAERRSHLEKYLR 1239
Cdd:cd07279    78 LIAERSRAFEQFLG 91
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 605-946 5.42e-09

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: 60.76  E-value: 5.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK 679
Cdd:pfam02463  163 AGSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   680 LKDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:pfam02463  243 QELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   755 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ 914
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578835464   915 YKERQLQYLLQNHLPTLLEEKQRAFEILDRGP 946
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 606-785 5.79e-09

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 60.35  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:pfam15709  347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQA 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   686 EKEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLEL 757
Cdd:pfam15709  417 AQERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEA 494

                          170       180
                   ....*....|....*....|....*...
gi 578835464   758 EKKRleEQEKEQVMLVahLEEQLREKQE 785
Cdd:pfam15709  495 EERR--QKEEEAARLA--LEEAMKQAQE 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-927 6.48e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 6.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ--QEVETQRKETEIVQLQIRKQEESLKRRSFhiENKLKDL 683
Cdd:TIGR02168  174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   684 LAEKEKFEEERLREQQEI-ELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKR 761
Cdd:TIGR02168  252 EEELEELTAELQELEEKLeELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   762 LEEQEKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEE 828
Cdd:TIGR02168  332 LDELAEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLER 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   829 LEKAQLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikp 908
Cdd:TIGR02168  412 LEDRRERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER--- 482

                          330
                   ....*....|....*....
gi 578835464   909 VEYRLQYKERQLQYLLQNH 927
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
605-1091 7.46e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.17  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  605 LRLEFERQQREELEKLESKRKlieemeEKQKSDKAELERMQQEVETQRKETEIVQlQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG4717    43 IRAMLLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLREQQEIELQKKRQE-----------EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYA 753
Cdd:COG4717   116 EELEKLEKLLQLLPLYQELEALEAElaelperleelEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  754 KLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIresLLRVKEARAGGDEDGEELEKAQ 833
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL---LLLIAAALLALLGLGGSLLSLI 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTEVPQDFEKIKPV 909
Cdd:COG4717   273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQEL 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  910 EYRLQYKERQLQyllqnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEftan 989
Cdd:COG4717   353 LREAEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLE---- 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  990 iarqeekvrKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLaslnsgsreqsglqASLEAEQE 1069
Cdd:COG4717   413 ---------ELLGELEELLEALDEEELEEELEELEEELEELEE------ELEELREEL--------------AELEAELE 463

                         490       500
                  ....*....|....*....|....
gi 578835464 1070 ALEKDQE--RLEYEIQQLKQKIYE 1091
Cdd:COG4717   464 QLEEDGElaELLQELEELKAELRE 487
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
611-1079 8.09e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 8.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 680
Cdd:PRK03918  269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  681 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:PRK03918  348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  761 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 840
Cdd:PRK03918  413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  841 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 916
Cdd:PRK03918  483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  917 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 992
Cdd:PRK03918  562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALE 1072
Cdd:PRK03918  638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717


                  ....*..
gi 578835464 1073 KDQERLE 1079
Cdd:PRK03918  718 KALERVE 724
PTZ00121 PTZ00121
MAEBL; Provisional
 611-1164 1.57e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 690
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  691 EEERLREQQEIELQKKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQv 770
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAE- 1460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  771 mlvaHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFEFKRrq 843
Cdd:PTZ00121 1461 ----EAKKKAEEAKKADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAEEAK-- 1534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  844 lvKLVNLEK-DLVQQKDILKK--EVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQL 920
Cdd:PTZ00121 1535 --KADEAKKaEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  921 QyllqnhlpTLLEEKQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniARQEEKVRKK 1000
Cdd:PTZ00121 1613 K--------KAEEAKIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKK-----------AEEENKIKAA 1664

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1001 EKEILESREKQQREALERALARLERRHSALQRHstlgmeiEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEY 1080
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1081 EIQQLKQKIYEVDGVQKDhhgtlEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTSADTMK 1160
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812


                  ....
gi 578835464 1161 DNEK 1164
Cdd:PTZ00121 1813 GGKE 1816
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 611-820 1.64e-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: 58.24  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG4942    26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  690 FEEE-----RLREQQEIELQKKRQEEETFLR--------VQEELQRLKELNNnEKAEKFQIFQELDQLQKEKDEQYAKLE 756
Cdd:COG4942   106 LAELlralyRLGRQPPLALLLSPEDFLDAVRrlqylkylAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELE 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835464  757 LEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLLRVKEARA 820
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 606-920 1.81e-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: 59.31  E-value: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLEskrklieemEEKQKSDKAELERMQQEVETQRKeteivqlQIRKQEESLKRrsfHIEnKLKDLLA 685
Cdd:TIGR02169  202 RLRREREKAERYQALL---------KEKREYEGYELLKEKEALERQKE-------AIERQLASLEE---ELE-KLTEEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLK-ELNNNEK--AEKFQIFQELDQLQKEKDEQYAKLELEKKRL 762
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   843 QLVKLVNLE---KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfEKIKPVEYRLQYKERQ 919
Cdd:TIGR02169  418 LSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK------EEYDRVEKELSKLQRE 491


                   .
gi 578835464   920 L 920
Cdd:TIGR02169  492 L 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
702-1212 2.82e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  702 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 781
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  782 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 858
Cdd:PRK03918  242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  859 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlPTLLEEKQRA 938
Cdd:PRK03918  321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-------GLTPEKLEKE 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  939 FEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIE 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1010 KQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLNSGSREQS--------GLQASLEAEQEALEKDQER- 1077
Cdd:PRK03918  473 EKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKKELEKl 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1078 --LEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMdariNAYIE--------EEVQRRLQDLHRV 1147
Cdd:PRK03918  552 eeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY----NEYLElkdaekelEREEKELKKLEEE 627

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835464 1148 ISEGCSTSADTMKDNEKLHNGTIQRKLKYEitvlDETWTvfRRYSRFREMHKTLKLKYAELAALE 1212
Cdd:PRK03918  628 LDKAFEELAETEKRLEELRKELEELEKKYS----EEEYE--ELREEYLELSRELAGLRAELEELE 686
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 1177-1240 2.95e-08

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 53.04  E-value: 2.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1177 EITVLDETWTVFRRYSRFREMHKTL-KLKYAELAAlEFPPKKLF--GNKDERVIAERRSHLEKYLRD 1240
Cdd:cd06897    21 QVRLPLRSYTVSRRYSEFVALHKQLeSEVGIEPPY-PLPPKSWFlsTSSNPKLVEERRVGLEAFLRA 86
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 1184-1239 4.07e-08

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 53.08  E-value: 4.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464 1184 TWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDER--VIAERRSHLEKYLR 1239
Cdd:cd06876    56 GWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQ 113
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 706-1079 4.49e-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: 57.77  E-value: 4.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   783 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 854
Cdd:TIGR02169  749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   855 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 934
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   935 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1012
Cdd:TIGR02169  887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464  1013 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALEKDQERLE 1079
Cdd:TIGR02169  960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAILERIEEYE 1013
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 623-907 4.64e-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: 57.77  E-value: 4.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   623 KRKLIEEM------EEKQKSDKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLR 696
Cdd:TIGR02169  155 RRKIIDEIagvaefDRKKEKALEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   697 EQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELE-KKRLEEQEKEQVMLVAH 775
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERS 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   776 LEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESLLRVKEARaggDEDGEELEKaqlrffefKRRQLVKLVNLEKDLV 855
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRR---DKLTEEYAE--------LKEELEDLRAELEEVD 377

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464   856 QQKDILKKEVQEEQEILECLKCEHD----KESRLLEKHDESVTDVTEVPQDFEKIK 907
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAIAGIE 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 706-1087 4.81e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   706 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 761
Cdd:TIGR02168  171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   762 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 841
Cdd:TIGR02168  251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   842 RQLVK-LVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 917
Cdd:TIGR02168  312 ANLERqLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   918 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 997
Cdd:TIGR02168  379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   998 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                          410
                   ....*....|.
gi 578835464  1077 RLEYEIQQLKQ 1087
Cdd:TIGR02168  500 NLEGFSEGVKA 510
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 1175-1238 5.14e-08

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 52.41  E-value: 5.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835464 1175 KYEITVLDETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNK-DERVIAERRSHLEKYL 1238
Cdd:cd06870    24 KVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNfDPDFIKQRRAGLDEFI 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 611-889 6.52e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   611 RQQREELEK-LESKRKLIEEMEEkqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:TIGR02168  711 EEELEQLRKeLEELSRQISALRK----DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   690 FEEERLREQQEIELQKKRQEE---------ETFLRVQEELQRLKelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDElraeltllnEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   761 RLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwvEEEKRDlEGIRESLLRVKEARAGGDEDGEELEKAQLRffefk 840
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRS------ELEELS-EELRELESKRSELRRELEELREKLAQLELR----- 930

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 578835464   841 rrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH 889
Cdd:TIGR02168  931 ------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
611-1083 8.81e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 8.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 690
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  691 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF----QELDQLQKEKDEQYAKLELEKKRLEEQE 766
Cdd:COG4717   152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEEL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  767 K--EQVMLVAHLEEQLREKQEMIQLLrrgevqwveeekrdleGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkrrQL 844
Cdd:COG4717   230 EqlENELEAAALEERLKEARLLLLIA----------------AALLALLGLGGSLLSLILTIAGVLFLVLGLL-----AL 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKhDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyll 924
Cdd:COG4717   289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQ--- 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  925 qnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEI 1004
Cdd:COG4717   365 ------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1005 LESRE--------KQQREALERALARLERRHSALQRhstlGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:COG4717   432 EELEEleeeleelEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507


                  ....*..
gi 578835464 1077 RLEYEIQ 1083
Cdd:COG4717   508 EYREERL 514
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 619-833 1.10e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.61  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  619 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 698
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  699 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 758
Cdd:COG3883    80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835464  759 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:COG3883   156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 706-1094 2.57e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  706 KRQEEETFLR---VQEELQRLK----ELNNN--------EKAEKFQifqELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 770
Cdd:COG1196   171 KERKEEAERKleaTEENLERLEdilgELERQleplerqaEKAERYR---ELKEELKELEAELLLLKLRELEAELEELEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  771 mlVAHLEEQLREKQEMIQLLRRgevqwveeekrdlegiresllRVKEARAGGDEDGEELEKAQLRFFEFKRRQLvklvnl 850
Cdd:COG1196   248 --LEELEAELEELEAELAELEA---------------------ELEELRLELEELELELEEAQAEEYELLAELA------ 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  851 ekDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDEsvtdvtevpqdfekikpveyrlqykerqlqyLLQNHLPT 930
Cdd:COG1196   299 --RLEQDIARLEERRRELEERLE----ELEEELAELEEELE-------------------------------ELEEELEE 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  931 LLEEKQRAFEILDrgplsldntlyqvekemeEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK 1010
Cdd:COG1196   342 LEEELEEAEEELE------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1011 QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIY 1090
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480


                  ....
gi 578835464 1091 EVDG 1094
Cdd:COG1196   481 ELLE 484
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 610-870 2.68e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 54.15  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   688 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 763
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 835
Cdd:pfam13868  181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 578835464   836 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 870
Cdd:pfam13868  261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 608-1088 3.26e-07

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: 54.97  E-value: 3.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQirkqeeslkRRSF 674
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHI---------KAVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   675 HIENKLKDLLAE-KEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQlQKEKDEQYA 753
Cdd:TIGR00618  304 QIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIH 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   754 KLELEKKRLEEQEKeqvmLVAHLEEQLREkqemiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:TIGR00618  383 TLQQQKTTLTQKLQ----SLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   834 LRFFEFKRRQLVKLVNLEKDLVQQKdilkkeVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRL 913
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQS------LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP------CPLCGSC 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   914 QYKERQLQYLLqnhlptLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQanaNQLQKLQATFEFTA----- 988
Cdd:TIGR00618  511 IHPNPARQDID------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---EQMQEIQQSFSILTqcdnr 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   989 -----NIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLnsgSREQSGLQAS 1063
Cdd:TIGR00618  582 skediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL---HALQLTLTQE 658

                          490       500
                   ....*....|....*....|....*
gi 578835464  1064 LEAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:TIGR00618  659 RVREHALSIRVLPKELLASRQLALQ 683
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.38e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                  ...
gi 578835464  549 FRF 551
Cdd:COG1716    91 LRF 93
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 1186-1238 5.34e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 49.63  E-value: 5.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1186 TVFRRYSRFREMHKTLKLKYAELAALE----FPPKKLFGNKDERVIAERRSHLEKYL 1238
Cdd:cd06881    39 VVWKRYSDFKKLHRELSRLHKQLYLSGsfppFPKGKYFGRFDAAVIEERRQAILELL 95
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
 1176-1240 5.50e-07

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 49.44  E-value: 5.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464 1176 YEITVLD---ETWTVFRRYSRFREMHKtlKLKYAELAALEFPPKKLFGNK-DERVIAERRSHLEKYLRD 1240
Cdd:cd06872    21 YSVAVTDnenETWVVKRRFRNFETLHR--RLKEVPKYNLELPPKRFLSSSlDGAFIEERCKLLDKYLKD 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-818 5.74e-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: 54.29  E-value: 5.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVqlqiRKQEESLKRRSFHIENKLKDLLA 685
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLER 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   686 EKEkfeeERLREQQEIELQKKRQEEEtflrvqeeLQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168  832 RIA----ATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578835464   766 EKEqvmlVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:TIGR02168  900 SEE----LRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQER 944
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 451-554 6.64e-07

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 49.61  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712     1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 578835464  512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712    76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
PTZ00121 PTZ00121
MAEBL; Provisional
 609-891 6.77e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  609 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdllA 685
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRVEIARKAEDARK----AEEARK---A 1172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  686 EKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKRLE 763
Cdd:PTZ00121 1173 EDAK------------KAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578835464  844 LVKlvNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:PTZ00121 1319 EAK--KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 608-819 6.78e-07

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: 53.92  E-value: 6.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI---RKQEESLKRRSFH-----IENK 679
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALNDLEARLSHsripeIQAE 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   680 LKDLlaEKEKFEEERLREQQEIELQKKRQEEETflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:TIGR02169  800 LSKL--EEEVSRIEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835464   760 KRLEEQEKEQVML---VAHLEEQLREKQEmiqllRRGEVQWVEEEKRDLEGIRESLLRVKEAR 819
Cdd:TIGR02169  875 AALRDLESRLGDLkkeRDELEAQLRELER-----KIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 605-891 7.91e-07

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: 53.82  E-value: 7.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLL 684
Cdd:pfam02463  726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEEL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   685 AEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRL 762
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELALELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEE 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ---------WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:pfam02463  879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekeneieeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464   834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:pfam02463  959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 612-1106 8.37e-07

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: 53.57  E-value: 8.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   612 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 672
Cdd:pfam05483  265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   673 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE 750
Cdd:pfam05483  345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   751 QyAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGD----EDG 826
Cdd:pfam05483  424 K-KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENK 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   827 EELEKAQLRFFEFKRRQlVKLVNLEKdlvqQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTdvTEVPQDFEKI 906
Cdd:pfam05483  503 ELTQEASDMTLELKKHQ-EDIINCKK----QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK--CKLDKSEENA 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   907 KPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQLAQYQANANQLQ-----K 979
Cdd:pfam05483  576 RSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLElelasA 648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   980 LQATFEFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQRHS-TLGMEIEEQRQKLA 1048
Cdd:pfam05483  649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALMEKHKhQYDKIIEERDSELG 728

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464  1049 SLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGK 1106
Cdd:pfam05483  729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
605-1091 8.77e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  605 LRLEFERQQREELEKLESKrklIEEMEEKQKSDKAELERMQQEVETQRKETEivqlqirkqeeslkrrsfHIENKLKDLL 684
Cdd:PRK02224  241 EVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLE------------------ELEEERDDLL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:PRK02224  300 AEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAELESELEEARE 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  765 QEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaqlrffefkrrql 844
Cdd:PRK02224  378 AVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE-------------- 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  845 VKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQL 920
Cdd:PRK02224  433 ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  921 QYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:PRK02224  502 EDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  999 KKEKEILESRE---KQQREALERALARLERRHSALQRHSTLgmeiEEQRQKLASLNSGSREQ--------SGLQASLEAE 1067
Cdd:PRK02224  571 REEVAELNSKLaelKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDERRERlaekrerkRELEAEFDEA 646

                         490       500
                  ....*....|....*....|....*
gi 578835464 1068 Q-EALEKDQERLEYEIQQLKQKIYE 1091
Cdd:PRK02224  647 RiEEAREDKERAEEYLEQVEEKLDE 671
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 611-787 1.15e-06

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: 51.08  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 690
Cdd:COG1579     3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  691 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:COG1579    79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                         170       180
                  ....*....|....*....|....*...
gi 578835464  760 KRLEEQEKEqvmLVAHLEEQLREKQEMI 787
Cdd:COG1579   159 EELEAEREE---LAAKIPPELLALYERI 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
614-990 1.29e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVET----QRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEK 689
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeaKAKKEELERLKKRLTGLTPEK----LEKELEELEKAKEE 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  690 FEEERLREQQEI-ELQKKRQEEETFLrvqEELQRLK--------ELNNNEKAEKFQIFQ-ELDQLQKEKDEQYAKLELEK 759
Cdd:PRK03918  403 IEEEISKITARIgELKKEIKELKKAI---EELKKAKgkcpvcgrELTEEHRKELLEEYTaELKRIEKELKEIEEKERKLR 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  760 KRLEEQEKE-----QVMLVAHLEEQLREKQEMiqlLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELE--KA 832
Cdd:PRK03918  480 KELRELEKVlkkesELIKLKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKK 556

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  833 QLRFFEFKRRQL-VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEH----DKESRLLEKHDESVTDVTEVPQDFEKIK 907
Cdd:PRK03918  557 KLAELEKKLDELeEELAELLKELEELGFESVEELEERLKELEPFYNEYlelkDAEKELEREEKELKKLEEELDKAFEELA 636

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  908 PVEYRLQYKERQLQYLLQNH-------LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:PRK03918  637 ETEKRLEELRKELEELEKKYseeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716

                         410
                  ....*....|
gi 578835464  981 QATFEFTANI 990
Cdd:PRK03918  717 EKALERVEEL 726
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
605-1143 1.87e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  605 LRLEFERQQREELEKLeskrklIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKL 680
Cdd:COG4913   281 LRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLEREL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  681 KDLLAEKEKFEEERLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:COG4913   355 EERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  761 RLEEQ----EKEQVMLVAHLEEQLREKQ-------EMIQLlRRGEVQW---VEeekRDLEGIRESLLrVKEARAggDE-- 824
Cdd:COG4913   430 SLERRksniPARLLALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaIE---RVLGGFALTLL-VPPEHY--AAal 502

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  825 ---DGEELeKAQLRFFEFK-RRQLVKLVNLEKD-LVQQKDI--------LKKEVQEEQEILeclKCEHDKEsrlLEKHDE 891
Cdd:COG4913   503 rwvNRLHL-RGRLVYERVRtGLPDPERPRLDPDsLAGKLDFkphpfrawLEAELGRRFDYV---CVDSPEE---LRRHPR 575

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  892 SVTdvtevpqdfekikpveyrlqyKERQLqyllqnHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekeEQLAQYQ 971
Cdd:COG4913   576 AIT---------------------RAGQV------KGNGTRHEKDDRRRIRSRYVLGFDNR------------AKLAALE 616

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  972 AnanQLQKLQATFEFTANIARQEekvrkkekeileSREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLN 1051
Cdd:COG4913   617 A---ELAELEEELAEAEERLEAL------------EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD 681

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1052 SGSREQSGLQ---ASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVAssslpvsAEKSHLVPLMDAR 1128
Cdd:COG4913   682 ASSDDLAALEeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-------LARLELRALLEER 754

                         570
                  ....*....|....*
gi 578835464 1129 INAYIEEEVQRRLQD 1143
Cdd:COG4913   755 FAAALGDAVERELRE 769
PTZ00121 PTZ00121
MAEBL; Provisional
 610-1243 4.66e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  610 ERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDllAEK 687
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD--AEE 1241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  688 EKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:PTZ00121 1242 AK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  768 --EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  844 LVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 919
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  920 LQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 996
Cdd:PTZ00121 1470 KK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  997 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQ----EALE 1072
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaEELK 1626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1073 KDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAE--KSHLVPLMDARINAYIEEEVQRRLQDLHRVISE 1150
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1151 GCSTSADTMKDNEKLHNGTIQRKLKYEITVLDETWTvfRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAE- 1229
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED--KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEe 1784

                         650       660
                  ....*....|....*....|.
gi 578835464 1230 -------RRSHLEKYLRDFFS 1243
Cdd:PTZ00121 1785 ldeedekRRMEVDKKIKDIFD 1805
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
 1169-1244 5.33e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 46.73  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1169 TIQRKLKYEITVL------DETWTVFRRYSRFREMHKTLKLKYAE-LAALEFPPKKLFGNKDERVIAERRSHLEKYLRDF 1241
Cdd:cd07300    14 TISKHVVYQIIVIqtgsfdCNKVVIERRYSDFLKLHQELLSDFSEeLEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLL 93


                  ...
gi 578835464 1242 FSV 1244
Cdd:cd07300    94 YSL 96
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
 1185-1238 5.69e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 46.98  E-value: 5.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464 1185 WTVFRRYSRFREMHKTLKLKYAELAALEFP--PKKLFGNKDERVIAERRSHLEKYL 1238
Cdd:cd06878    50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYL 105
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 610-803 6.11e-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: 50.15  E-value: 6.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRR-----SFHIENKLKDLL 684
Cdd:COG4942    47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKEKDEQYAKLEL 757
Cdd:COG4942   127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAERQKLLARLEK 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578835464  758 EKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG4942   207 ELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 1157-1240 6.75e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 46.07  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1157 DTMKDNEKLH-NGTIQRKLKYEITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLE 1235
Cdd:cd06866     1 DTVTVELVPEkKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLS 80


                  ....*
gi 578835464 1236 KYLRD 1240
Cdd:cd06866    81 RFLNL 85
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
627-782 8.63e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.24  E-value: 8.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  627 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 706
Cdd:COG2433   382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464  707 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:COG2433   454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKE 522
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 471-555 1.20e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 44.94  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 578835464   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
607-1095 1.22e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAE 686
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  687 KEKFEEERLREQQEIELQKKRQEEetflRVQEELQRLKELNNNEKaekfqifqELDQLqKEKDEQYAKLELE----KKRL 762
Cdd:PRK03918  243 LEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKVK--------ELKEL-KEKAEEYIKLSEFyeeyLDEL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  763 EEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEARAGGDE--------DGEE 828
Cdd:PRK03918  310 REIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEElerlkkrlTGLT 385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  829 LEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-------------CEHDKEsRLLEKHDESVTD 895
Cdd:PRK03918  386 PEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelTEEHRK-ELLEEYTAELKR 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  896 VTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEIldrgpLSLDNTLYQVekemeekeeqlaqyqaNAN 975
Cdd:PRK03918  464 IEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQL-----KELEEKLKKY----------------NLE 518

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  976 QLQKLQATFEFTANIARQEEKVRKKEKEILESRE--KQQREALERALARLERRHSALQRH-STLGME-IEEQRQKLASLN 1051
Cdd:PRK03918  519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKElEELGFEsVEELEERLKELE 598

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 578835464 1052 SGSREQSGLQASlEAEQEALEKDQERLEYEIQQLKQKIYEVDGV 1095
Cdd:PRK03918  599 PFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKR 641
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 608-806 1.47e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 49.18  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLKRrsfhiENKLkdllaeK 687
Cdd:pfam15709  312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLER-----AEKM------R 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   688 EKFEEERLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKEKDEQYA-KLELEKKRLE 763
Cdd:pfam15709  376 EELELEQQRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRKKQQEEAeRAEAEKQRQK 455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578835464   764 EQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 806
Cdd:pfam15709  456 ELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 799-1100 1.64e-05

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: 49.67  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   799 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 877
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   878 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH------LPTLLEEKQRAFEILDRGPLSLDN 951
Cdd:TIGR02168  246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEA 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   952 TLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarQEEKVRKKEKEILESREKQQREALERA------------ 1019
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLrskvaqlelqia 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  1020 -----LARLERRHSALQ-RHSTLGMEIEEQRQKL--ASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1091
Cdd:TIGR02168  397 slnneIERLEARLERLEdRRERLQQEIEELLKKLeeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476


                   ....*....
gi 578835464  1092 VDGVQKDHH 1100
Cdd:TIGR02168  477 LDAAERELA 485
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 576-906 2.03e-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: 48.95  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   576 MTDLSKSRENLSAVMLynpglfPIKGPICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKET 655
Cdd:pfam05483  337 MEELNKAKAAHSFVVT------EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   656 EIV------QLQIRKQEESLKRRSFHIENKLKDLLAEKEKfeeerLREQQEIELQKKRQEEETFLRVQEELQRLKElnnN 729
Cdd:pfam05483  411 KKIlaedekLLDEKKQFEKIAEELKGKEQELIFLLQAREK-----EIHDLEIQLTAIKTSEEHYLKEVEDLKTELE---K 482

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   730 EKAEKFQIFQELDqlqkekdeqyaKLELEKKRLEEQEKEQVM-LVAHLEEQLREKQEMIQLLRRGE-VQWVEEEKRD-LE 806
Cdd:pfam05483  483 EKLKNIELTAHCD-----------KLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIEnLEEKEMNLRDeLE 551

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   807 GIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLL 886
Cdd:pfam05483  552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631

                          330       340
                   ....*....|....*....|....
gi 578835464   887 EKHDESVT----DVTEVPQDFEKI 906
Cdd:pfam05483  632 NAYEIKVNklelELASAKQKFEEI 655
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 612-1085 3.26e-05

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: 48.43  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   612 QQREELEKLESKRKLIEEMEEK--QKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:TIGR00618  264 QLRARIEELRAQEAVLEETQERinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   690 FEEERLREQQEIELQKKRQEEETFL----RVQEELQRLKELNNNEKA--EKFQIF-QELDQLQKEKDEQYAKL------- 755
Cdd:TIGR00618  344 RRLLQTLHSQEIHIRDAHEVATSIReiscQQHTLTQHIHTLQQQKTTltQKLQSLcKELDILQREQATIDTRTsafrdlq 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   756 ----------ELEKKRLEEQE-------KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWV-EEEKRDLEGIRESLLRVKE 817
Cdd:TIGR00618  424 gqlahakkqqELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLqETRKKAVVLARLLELQEEP 503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   818 ARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCE----HDKESRLLEKHDESV 893
Cdd:TIGR00618  504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeiQQSFSILTQCDNRSK 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   894 TDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEkqrafeildrgplsLDNTLYQVEKEMEEKEEQLAQYQAN 973
Cdd:TIGR00618  584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE--------------QDLQDVRLHLQQCSQELALKLTALH 649

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   974 ANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslNSG 1053
Cdd:TIGR00618  650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE--NAS 727

                          490       500       510
                   ....*....|....*....|....*....|..
gi 578835464  1054 SREQSGLQASLEAEQEALEKDQERLEYEIQQL 1085
Cdd:TIGR00618  728 SSLGSDLAAREDALNQSLKELMHQARTVLKAR 759
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 651-843 3.31e-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: 46.84  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  651 QRKETEIVQlqIRKQEESLKRRsfhiENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLrVQEELQRLKELNNNE 730
Cdd:COG1579    13 QELDSELDR--LEHRLKELPAE----LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-VEARIKKYEEQLGNV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  731 KAEKfqifqELDQLQKEKDeqyaKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRE 810
Cdd:COG1579    86 RNNK-----EYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 578835464  811 SLLRVKEARAggdEDGEELEKAQLRFFEFKRRQ 843
Cdd:COG1579   157 ELEELEAERE---ELAAKIPPELLALYERIRKR 186
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 602-1024 4.87e-05

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: 48.04  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   602 PICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLK 681
Cdd:pfam02463  603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK----ELLEI 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   682 DLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyAKLELEKKR 761
Cdd:pfam02463  679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE--EEEEEEKSR 756

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   762 LEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFfEFKR 841
Cdd:pfam02463  757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK-EEEL 835

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   842 RQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT-DVTEVPQDFEKIKPVEYRLQYK--ER 918
Cdd:pfam02463  836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSKEEKEKEEKKELEEESQKLNLleEK 915

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   919 QLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:pfam02463  916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995

                          410       420
                   ....*....|....*....|....*.
gi 578835464   999 KKEKEILESREKQQREALERALARLE 1024
Cdd:pfam02463  996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 613-870 5.03e-05

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 47.34  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   613 QREELEKLESKRKLIEEmEEKQKSDKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSFHI---ENKLKDLLAEKEK 689
Cdd:pfam15558   33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKARLG------REERRRADRREKQViekESRWREQAEDQEN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   690 FEEERLREQQEIELQKKRQEEETfLRVQEE-LQRLKELNNNEKAEKFQI---------------FQELDQ---------- 743
Cdd:pfam15558  106 QRQEKLERARQEAEQRKQCQEQR-LKEKEEeLQALREQNSLQLQERLEEachkrqlkereeqkkVQENNLsellnhqark 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   744 ----LQKEKDEQYAKLELEKKRLEEQEK-EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKE 817
Cdd:pfam15558  185 vlvdCQAKAEELLRRLSLEQSLQRSQENyEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELAD 261

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578835464   818 ARAGGDEDGEELEKAQlrffefkRRQLVKLVNLEKDLVQQkdILKKEVQEEQE 870
Cdd:pfam15558  262 RKIQQARQVAHKTVQD-------KAQRARELNLEREKNHH--ILKLKVEKEEK 305
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
909-1096 7.83e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 7.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  909 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:COG3206   162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  981 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSAlqRHStlgmEIEEQRQKLASLNSG-SREQSG 1059
Cdd:COG3206   242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHP----DVIALRAQIAALRAQlQQEAQR 313

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578835464 1060 LQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQ 1096
Cdd:COG3206   314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
PRK12704 PRK12704
phosphodiesterase; Provisional
 613-768 8.18e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 8.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  613 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 692
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464  693 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:PRK12704  122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
 1182-1253 9.35e-05

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 43.11  E-value: 9.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835464 1182 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERR-SHLEKYLRDFFSVMLQSATSPL 1253
Cdd:cd06883    29 TEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRkIELNSYLKSLFNASPEVAESDL 101
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 612-1105 9.76e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.09  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   612 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 691
Cdd:pfam01576    2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   692 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 748
Cdd:pfam01576   63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   749 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 805
Cdd:pfam01576  134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   806 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 867
Cdd:pfam01576  214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   868 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 940
Cdd:pfam01576  294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   941 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:pfam01576  367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  1010 KQQREAlERALARLERRHSAL--QRHSTLGMEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEAlekdQERLEYEIQQ 1084
Cdd:pfam01576  447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEA----KRNVERQLST 521

                          570       580
                   ....*....|....*....|.
gi 578835464  1085 LKQKIYEVDGVQKDHHGTLEG 1105
Cdd:pfam01576  522 LQAQLSDMKKKLEEDAGTLEA 542
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 615-831 1.31e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   615 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 694
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   695 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 774
Cdd:TIGR02169  892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835464   775 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 831
Cdd:TIGR02169  955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1008-1212 1.52e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1008 REKQQREALERALARLERRHSALQRHSTL-----GMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEI 1082
Cdd:COG4913   246 DAREQIELLEPIRELAERYAAARERLAELeylraALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1083 QQLKQKIYEVDGVQKDHhgtLEGKVAssslpvSAEKSHlvplmdarinayieEEVQRRLQDLH---RVISEGCSTSADTM 1159
Cdd:COG4913   326 DELEAQIRGNGGDRLEQ---LEREIE------RLEREL--------------EERERRRARLEallAALGLPLPASAEEF 382

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578835464 1160 KDNEKLHNGTIQRKLKYEITVLDETWTVFRRYSRFREMHKTLKlkyAELAALE 1212
Cdd:COG4913   383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE---AEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-1117 2.02e-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: 45.82  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQ--------IRKQEESLKRRSFHIE 677
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEELQEELERLE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   678 NKLKDLLAEKEKFEEERLREQQeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQK--EKDEQYAK- 754
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAER--ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEliSVDEGYEAa 538

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   755 ----------------LELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMIQLLRRGEVQW---VEEEKRDLEGIR 809
Cdd:TIGR02168  539 ieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLdsikgtEIQGNDREILKNIEGFLGVakdLVKFDPKLRKAL 618

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   810 ESLL-------RVKEA---------------------RAGGDEDGEELEKAQLRFfeFKRRQLVKLVNLEKDLVQQKDIL 861
Cdd:TIGR02168  619 SYLLggvlvvdDLDNAlelakklrpgyrivtldgdlvRPGGVITGGSAKTNSSIL--ERRREIEELEEKIEELEEKIAEL 696

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   862 KKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRA 938
Cdd:TIGR02168  697 EKALAElRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeiEELEERLEEAEEE 776

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   939 FEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALER 1018
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  1019 ALARLE-------RRHSALQRHSTLGMEIEEQRQKL--------ASLNSGSREQSGLQASLEAEQEALEK---DQERLEY 1080
Cdd:TIGR02168  857 LAAEIEeleelieELESELEALLNERASLEEALALLrseleelsEELRELESKRSELRRELEELREKLAQlelRLEGLEV 936

                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 578835464  1081 EIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAE 1117
Cdd:TIGR02168  937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 605-1149 2.15e-04

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: 45.98  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDL 683
Cdd:pfam12128  380 RRSKIKEQNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   684 LAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam12128  457 TATPE-------------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLE 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   764 EQEKEqvmlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeF 839
Cdd:pfam12128  517 ERQSA----LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---L 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   840 KRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam12128  588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQS 664

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   920 LQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTAN 989
Cdd:pfam12128  665 EKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSG 744

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   990 IARQEEKVRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGMEIE 1041
Cdd:pfam12128  745 AKAELKALETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAIS 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  1042 EQRQKLASLNSGSREQsglQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDhhgtleGKVASSSLPVSAEKSHL 1121
Cdd:pfam12128  825 ELQQQLARLIADTKLR---RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED------ANSEQAQGSIGERLAQL 895

                          570       580
                   ....*....|....*....|....*...
gi 578835464  1122 VPLMDarINAYIEEEVQRRLQDLHRVIS 1149
Cdd:pfam12128  896 EDLKL--KRDYLSESVKKYVEHFKNVIA 921
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 607-873 2.27e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 686
Cdd:pfam13868   91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   687 KEKFEeerlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 766
Cdd:pfam13868  168 EEERE------------AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   767 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 846
Cdd:pfam13868  232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308

                          250       260
                   ....*....|....*....|....*..
gi 578835464   847 LVNLEkdlVQQKDILKKEVQEEQEILE 873
Cdd:pfam13868  309 EREEE---LEEGERLREEEAERRERIE 332
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 1189-1244 2.50e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 41.63  E-value: 2.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464 1189 RRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAeRRSHLEKYLRDFFSV 1244
Cdd:cd06886    36 RRYREFANLHQNLKKEFPDFQFPKLPGKWPFSLSEQQLDA-RRRGLEQYLEKVCSI 90
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 852-1089 2.57e-04

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: 44.75  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  852 KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpqdfeKIKPVEYRLQYKERQLQyllqnhlpTL 931
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR------RIRALEQELAALEAELA--------EL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  932 LEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK- 1010
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAe 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1011 --QQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGsreqsglQASLEAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:COG4942   169 leAERAELEALLAELEEERAALEA------LKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIARLEAE 235


                  .
gi 578835464 1089 I 1089
Cdd:COG4942   236 A 236
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 473-551 2.60e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 41.43  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673    18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93


                  .
gi 578835464  551 F 551
Cdd:cd22673    94 F 94
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 1190-1238 2.60e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 41.55  E-value: 2.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578835464 1190 RYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERvIAERRSHLEKYL 1238
Cdd:cd06885    34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQ-LEERRLQLEKYL 81
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 1176-1238 2.80e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 41.49  E-value: 2.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835464 1176 YEITVLDE--TWTVFRRYSRFREMHKTLKLKYaelAALEFPPKKLfGNKDERVIAERRSHLEKYL 1238
Cdd:cd06880    22 FTIEVLVNgrRHTVEKRYSEFHALHKKLKKSI---KTPDFPPKRV-RNWNPKVLEQRRQGLEAYL 82
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 478-543 2.91e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 40.25  E-value: 2.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464   478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 1169-1240 2.93e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 41.98  E-value: 2.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464 1169 TIQRKLKYEITVLDETWTVFRRYSRFRemhkTLKLKYAE----LAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1240
Cdd:cd06877    28 EVERNDRRAKGHEPQHWSVLRRYNEFY----VLESKLTEfhgeFPDAPLPSRRIFGPKSYEFLESKREIFEEFLQK 99
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 608-902 4.07e-04

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: 45.04  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEEK----------QKSDKAELERMQQEVETQRKET-EIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606  238 EIVKSYENELDPLKNRLKEIEHNLSKimkldneikaLKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREK 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   677 ENKLKDLLAEKEKFEEERLreqqeiELQKKRQE---EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKD---E 750
Cdd:TIGR00606  318 ERELVDCQRELEKLNKERR------LLNQEKTEllvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFserQ 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   751 QYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLLRVKearaggdEDGE 827
Cdd:TIGR00606  392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekKGLGRTIELKKEILEKKQEELKFVI-------KELQ 464

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464   828 ELEKAQLRFFEFK---RRQLVKLVNLEKD-LVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 902
Cdd:TIGR00606  465 QLEGSSDRILELDqelRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD 543
COG5022 COG5022
Myosin heavy chain [General function prediction only];
611-867 4.70e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG5022   806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  685 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 748
Cdd:COG5022   880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 828
Cdd:COG5022   953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578835464  829 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 867
Cdd:COG5022  1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
611-803 4.82e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEk 687
Cdd:COG1340    95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  688 ekfeeerlreqqeieLQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1340   169 ---------------LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 578835464  768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG1340   231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 720-1091 5.94e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 5.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   720 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 797
Cdd:pfam17380  278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   798 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEeqeilecl 875
Cdd:pfam17380  353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQR-------- 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   876 kcehdkesrlleKHDESVTDVTEVPQDFEKIKPVEYRL--QYKERQLQYLLQNHLptlleEKQRAFEILdrgplsldntl 953
Cdd:pfam17380  414 ------------KIQQQKVEMEQIRAEQEEARQREVRRleEERAREMERVRLEEQ-----ERQQQVERL----------- 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   954 yqvekemeekeeqlaqyqananqlqklqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRH 1033
Cdd:pfam17380  466 --------------------------------------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRR 494

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464  1034 STLGMEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1091
Cdd:pfam17380  495 KILEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
PRK12704 PRK12704
phosphodiesterase; Provisional
 676-820 6.85e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  676 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 751
Cdd:PRK12704   36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464  752 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 820
Cdd:PRK12704  102 LELLEKREEELEKKEKE----LEQKQQELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 614-924 6.88e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQrkETEIVQLQIR-----KQEESLKRRSFHIEN------KLKD 682
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKLRSRvdlklQELQHLKNEGDHLRNvqteceALKL 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   683 LLAEKEKFeeerlreqqeIELQKKRQEEETFLRVQ----------EELQRLKELNNNEkaekfqifQELDQLQKEKDEQY 752
Cdd:pfam15921  556 QMAEKDKV----------IEILRQQIENMTQLVGQhgrtagamqvEKAQLEKEINDRR--------LELQEFKILKDKKD 617

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   753 AKLELEKKRLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEVQWVEEE----KRDLEGIRESL------- 812
Cdd:pfam15921  618 AKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSEDyevlKRNFRNKSEEMetttnkl 697

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   813 -LRVKEARAggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK---DILKKEVQ-EEQEILECLKCEH---DK 881
Cdd:pfam15921  698 kMQLKSAQS-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgqiDALQSKIQfLEEAMTNANKEKHflkEE 770

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 578835464   882 ESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:pfam15921  771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 703-908 8.14e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.45  E-value: 8.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 781
Cdd:pfam05262  183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   782 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 861
Cdd:pfam05262  256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 578835464   862 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 908
Cdd:pfam05262  309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
 1186-1242 8.23e-04

The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 40.72  E-value: 8.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1186 TVFRRYSRFREMHKTLKLKYAELAALE--FPP---KKLFGNKDERVIAERRSHLE---------------KYLRDFF 1242
Cdd:cd07287    39 VVWKRYSDFKKLHKDLWQIHKNLCRQSelFPPfakAKVFGRFDESVIEERRQCAEdllqfsanipalynsSQLEDFF 115
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 605-764 8.54e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRL 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   685 AEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQIFQELDQLQKEKDEQY 752
Cdd:TIGR02169  920 SELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QEYEEVLKRLDELKEKR 995

                          170
                   ....*....|..
gi 578835464   753 AKLELEKKRLEE 764
Cdd:TIGR02169  996 AKLEEERKAILE 1007
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
598-832 9.51e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  598 PIKG-PICLRLEFERQQREELE-KLESKRKLIEEMEEK--QKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRS 673
Cdd:PRK02224  460 PVEGsPHVETIEEDRERVEELEaELEDLEEEVEEVEERleRAEDLVEAED---RIERLEERREDLEELIAERRETIEEKR 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  674 FHIENKLK---DLLAEKEkfeeerlreqqeielQKKRQEEETFLRVQEELQRLKELNnnekAEKFQIFQELDQLQK--EK 748
Cdd:PRK02224  537 ERAEELREraaELEAEAE---------------EKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERirTL 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrRGEVQ--WVEEEKRDLEGIRESLLRVKEARAGGDEDG 826
Cdd:PRK02224  598 LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKREL-EAEFDeaRIEEAREDKERAEEYLEQVEEKLDELREER 676


                  ....*.
gi 578835464  827 EELEKA 832
Cdd:PRK02224  677 DDLQAE 682
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 551-820 9.58e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  551 FNHPKEAAKLREKRKSgllssfslsMTDLSKSRENLSAVMLYNPGLFPIKGPICLR--LEFERQQREELEKLESKrklIE 628
Cdd:PRK05771   36 LKEELSNERLRKLRSL---------LTKLSEALDKLRSYLPKLNPLREEKKKVSVKslEELIKDVEEELEKIEKE---IK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  629 EMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI-ENKLKDLLAEKEKFEEERLREQQE-- 700
Cdd:PRK05771  104 ELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVpEDKLEELKLESDVENVEYISTDKGyv 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  701 --IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE 778
Cdd:PRK05771  180 yvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578835464  779 QL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 820
Cdd:PRK05771  255 YLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
 1187-1239 1.14e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 40.34  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464 1187 VFRRYSRFREMHKTLKLKYAEL--AALEFPP---KKLFGNKDERVIAERRSHLEKYLR 1239
Cdd:cd07288    40 VWKRYSDLKKLHGELAYTHRNLfrRQEEFPPfprAQVFGRFEAAVIEERRNAAEAMLL 97
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 452-554 1.26e-03

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 39.78  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 578835464  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 608-713 1.30e-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: 42.83  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4942   143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                          90       100
                  ....*....|....*....|....*.
gi 578835464  688 EKFEEERLREQQEIELQKKRQEEETF 713
Cdd:COG4942   223 EELEALIARLEAEAAAAAERTPAAGF 248
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 1176-1233 1.39e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 39.70  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578835464 1176 YEITVL---DETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNKDERVIAERRSH 1233
Cdd:cd07276    23 YKIRVEnkvGDSWFVFRRYTDFVRLNDKLKQMFPGF-RLSLPPKRWFKDNFDPDFLEERQL 82
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 608-763 1.40e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam17380  447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464   688 EKFEEERLREQQEIELQKKR---QEEETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam17380  523 EERQKAIYEEERRREAEEERrkqQEMEERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 608-829 1.59e-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: 42.85  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 675
Cdd:pfam01576  163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   676 IENKLKDLLAEKEKFEEERLREqqeieLQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDEQ 751
Cdd:pfam01576  241 KEEELQAALARLEEETAQKNNA-----LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDTT 315

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464   752 YAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEEL 829
Cdd:pfam01576  316 AAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 605-938 1.79e-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: 42.50  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQEVETQ-------RKETEIVQLQIR---KQEESLKRRSF 674
Cdd:pfam10174  350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRdkdKQLAGLKERVK 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   675 HIEN----------KLKDLLAEKEKFEEERLREqQEIELQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQL 744
Cdd:pfam10174  426 SLQTdssntdtaltTLEEALSEKERIIERLKEQ-REREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   745 QK----------EKDEQYAKLE--LEKKRLEEQEKEQVMLVAH-LEEQLREKQEM---IQLLRRgEVQWVEEEKR----D 804
Cdd:pfam10174  502 KEhasslassglKKDSKLKSLEiaVEQKKEECSKLENQLKKAHnAEEAVRTNPEIndrIRLLEQ-EVARYKEESGkaqaE 580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   805 LEGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkRRQLVKLVNLEkdLVQQKDiLKKEVQEEQEILECLKCEHDKESR 884
Cdd:pfam10174  581 VERLLGILREVENEKNDKDKKIAELESLTLRQM---KEQNKKVANIK--HGQQEM-KKKGAQLLEEARRREDNLADNSQQ 654

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578835464   885 LleKHDESVTDVTEVPQDFEKIK----PVEYRLQYKERQLQYLLQN---HLPTLLEEKQRA 938
Cdd:pfam10174  655 L--QLEELMGALEKTRQELDATKarlsSTQQSLAEKDGHLTNLRAErrkQLEEILEMKQEA 713
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 611-988 1.79e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 678
Cdd:TIGR04523  267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   679 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 757
Cdd:TIGR04523  343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   758 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 836
Cdd:TIGR04523  420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   837 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQE---EQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 913
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835464   914 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 988
Cdd:TIGR04523  564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612
Caldesmon pfam02029
Caldesmon;
608-873 1.93e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 683
Cdd:pfam02029   10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   684 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029   83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   764 EQEKEQVMLVAHLEEQLRE---------KQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam02029  163 SEEAEEVPTENFAKEEVKDekikkekkvKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578835464   829 LEKAQLRfFEFKRRQLVKLVNLEKDLVQQK--------DILKKEVQEEQEILE 873
Cdd:pfam02029  243 FLEAEQK-LEELRRRRQEKESEEFEKLRQKqqeaelelEELKKKREERRKLLE 294
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 606-921 2.49e-03

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: 41.80  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   606 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEE---SLKRRSFH 675
Cdd:pfam07888   68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   676 IENKLKDLLAEKEKFEEerlreqqeielQKKRQEEEtflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL 755
Cdd:pfam07888  148 RETELERMKERAKKAGA-----------QRKEEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   756 ELEKKRLEEQEKEQVMLVAHLE---EQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRE-SLLRVKEARAGGDEDGEELEK 831
Cdd:pfam07888  212 QDTITTLTQKLTTAHRKEAENEallEELRSLQERLNASER-KVEGLGEELSSMAAQRDrTQAELHQARLQAAQLTLQLAD 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   832 AQLRFFEFK------RRQLVKLVNLEKDLVQQkdiLKKEVQEEQEILECLKCEHDK-ESRLLEKHDESVTDVTEVPQDFE 904
Cdd:pfam07888  291 ASLALREGRarwaqeRETLQQSAEADKDRIEK---LSAELQRLEERLQEERMEREKlEVELGREKDCNRVQLSESRRELQ 367

                          330
                   ....*....|....*..
gi 578835464   905 KIKPVEYRLQYKERQLQ 921
Cdd:pfam07888  368 ELKASLRVAQKEKEQLQ 384
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 602-867 2.61e-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: 42.34  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   602 PICLR-LEFERQQREELEKLESKRKLieeMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKL 680
Cdd:TIGR00606  681 PVCQRvFQTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   681 KDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQrlKELNNNEKAEKFQI-----------FQELDQLQKEKD 749
Cdd:TIGR00606  758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ--MELKDVERKIAQQAaklqgsdldrtVQQVNQEKQEKQ 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   750 EQY----AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:TIGR00606  836 HELdtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQDSPL 914

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 578835464   826 GEELEKAQLRffefkRRQLVKLVNLEKDLVQQK-DILKKEVQE 867
Cdd:TIGR00606  915 ETFLEKDQQE-----KEELISSKETSNKKAQDKvNDIKEKVKN 952
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
 1186-1252 2.77e-03

The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132778  Cd Length: 120  Bit Score: 38.93  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1186 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFgnKDERVIAERRSHLEKYLRdFFSVMLQSATSP 1252
Cdd:cd06868    48 MVSKKYSEFEELYKKLSEKYPGTILPPLPRKALF--VSESDIRERRAAFNDFMR-FISKDEKLANCP 111
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 704-888 2.87e-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: 41.67  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE---QYAKLELEKKRLEEQEKEQVMLVAHLEEQL 780
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  781 REKQEMI--------------------------QLLRRGEV--QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkA 832
Cdd:COG4942   100 EAQKEELaellralyrlgrqpplalllspedflDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELE-A 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464  833 QLRFFEFKRRQLVKLVNLEKDLVQQkdiLKKEVQEEQEILECLKCEHDKESRLLEK 888
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIAR 231
PRK12704 PRK12704
phosphodiesterase; Provisional
 624-788 2.99e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  624 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 703
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 778
Cdd:PRK12704   89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165

                         170
                  ....*....|.
gi 578835464  779 QLR-EKQEMIQ 788
Cdd:PRK12704  166 EARhEAAVLIK 176
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 605-764 3.18e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   605 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRsfhienklkdlL 684
Cdd:pfam05672   23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQR-----------K 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   685 AEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 764
Cdd:pfam05672   81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 611-689 3.19e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835464  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG3883   129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
Caldesmon pfam02029
Caldesmon;
608-786 3.54e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   608 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 687
Cdd:pfam02029  147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   688 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029  223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301

                          170       180
                   ....*....|....*....|...
gi 578835464   764 EQEKEQvmLVAHLEEQLREKQEM 786
Cdd:pfam02029  302 QEEAER--KLREEEEKRRMKEEI 322
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 706-1096 3.61e-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: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQEL----DQLQKEKDEQYAKLELEKKRLEEQE--KEQVMLVAH---- 775
Cdd:pfam15921   77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVidlqTKLQEMQMERDAMADIRRRESQSQEdlRNQLQNTVHelea 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   776 ----LEEQLREKQEMIQLLRRGEVQwveeEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLE 851
Cdd:pfam15921  157 akclKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTE 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   852 KDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTE----VPQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam15921  233 ISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEkassARSQANSIQSQLEIIQEQARN 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   920 LQYLLQNHLPTL----------LEEKQRAFE----------ILDRGPLS---------------LDNTLYQVEKEMEEKE 964
Cdd:pfam15921  311 QNSMYMRQLSDLestvsqlrseLREAKRMYEdkieelekqlVLANSELTearterdqfsqesgnLDDQLQKLLADLHKRE 390

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   965 EQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRHSTLGMEI 1040
Cdd:pfam15921  391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQL 470

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835464  1041 EEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALE-------KDQERLEYEIQQLKQKIYEVDGVQ 1096
Cdd:pfam15921  471 ESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSRVDLKLQELQHLKNEGDHLR 544
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 607-869 3.76e-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: 41.65  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   607 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:pfam05557   43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   687 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 759
Cdd:pfam05557  116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   760 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam05557  179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464   829 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQ 869
Cdd:pfam05557  254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLE 310
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 1186-1239 4.37e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 38.33  E-value: 4.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578835464 1186 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERV--IAERRSHLEKYLR 1239
Cdd:cd06859    38 SVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVKFefIEKRRAALERFLR 93
46 PHA02562
endonuclease subunit; Provisional
 618-861 4.52e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  618 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 697
Cdd:PHA02562  195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  698 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 773
Cdd:PHA02562  268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  774 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 849
Cdd:PHA02562  328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393

                         250
                  ....*....|..
gi 578835464  850 LEKDLVQQKDIL 861
Cdd:PHA02562  394 TKSELVKEKYHR 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 615-768 4.56e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   615 EELEKL-ESKRKLIEEMEEKQKSDKAELERMQQEVEtqRKETEIVQLQIRKQE-------------------ESLKRRSF 674
Cdd:TIGR04523  457 KNLDNTrESLETQLKVLSRSINKIKQNLEQKQKELK--SKEKELKKLNEEKKEleekvkdltkkisslkekiEKLESEKK 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   675 HIENKLKDLLAEKEKFEEERLREQQEIELQKKrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:TIGR04523  535 EKESKISDLEDELNKDDFELKKENLEKEIDEK----------NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604

                          170
                   ....*....|....
gi 578835464   755 LELEKKRLEEQEKE 768
Cdd:TIGR04523  605 IEEKEKKISSLEKE 618
Caldesmon pfam02029
Caldesmon;
621-772 4.66e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   621 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 700
Cdd:pfam02029  206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835464   701 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 772
Cdd:pfam02029  279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 1183-1243 4.72e-03

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 38.57  E-value: 4.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1183 ETWTVFRRYSRFREMHKTLKLKY---AELAAL-----EFPPKKLFGNKDErvIAERR-SHLEKYLRDFFS 1243
Cdd:cd06882    33 SKYLIYRRYRQFFALQSKLEERFgpeAGSSAYdctlpTLPGKIYVGRKAE--IAERRiPLLNRYMKELLS 100
PX_SNX21 cd07301
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ...
 1189-1244 4.77e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132834  Cd Length: 112  Bit Score: 38.25  E-value: 4.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578835464 1189 RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSV 1244
Cdd:cd07301    40 RRYSDFERLHRRLRRLFgGEMAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSL 96
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 757-1091 4.95e-03

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: 41.03  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   757 LEKKRLEEQEKEQVMLV--------AHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESL-LRVKEARAGGDEDGE 827
Cdd:pfam07888    9 LEEESHGEEGGTDMLLVvpraellqNRLEECLQERAELLQAQEAANRQ-REKEKERYKRDREQWeRQRRELESRVAELKE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   828 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQE-EQEILEclkCEHDKESrLLEKHDESVTDVTEVPQDFEKI 906
Cdd:pfam07888   88 ELRQSREKHEELEEKY-KELSASSEELSEEKDALLAQRAAhEARIRE---LEEDIKT-LTQRVLERETELERMKERAKKA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   907 KPVEYRLQYKERQLQYLLQ------NHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:pfam07888  163 GAQRKEEEAERKQLQAKLQqteeelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   981 QATFeftaNIARQEEKVRKKEKEILESREKQQREALERalARLERRHSALQRhSTLGMEIEEQRQKLAslnsgsREQSGL 1060
Cdd:pfam07888  243 QERL----NASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQL-ADASLALREGRARWA------QERETL 309

                          330       340       350
                   ....*....|....*....|....*....|.
gi 578835464  1061 QASLEAEQEALEKdqerLEYEIQQLKQKIYE 1091
Cdd:pfam07888  310 QQSAEADKDRIEK----LSAELQRLEERLQE 336
RNase_Y_N pfam12072
RNase Y N-terminal region;
623-768 6.65e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   623 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 702
Cdd:pfam12072   52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835464   703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:pfam12072  120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 618-818 7.38e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269    87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464  698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHL 776
Cdd:cd16269   155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578835464  777 EEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269   229 EDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 611-727 9.30e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.13  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464   611 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 688
Cdd:pfam09731  319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 578835464   689 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 727
Cdd:pfam09731  390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1010-1119 9.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835464 1010 KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1089
Cdd:COG3883   139 KADKAELEAKKAELEAKLAELEA------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

                          90       100       110
                  ....*....|....*....|....*....|
gi 578835464 1090 YEVDGVQKDHHGTLEGKVASSSLPVSAEKS 1119
Cdd:COG3883   213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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