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Conserved domains on  [gi|112734867|ref|NP_065099.3|]
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X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 [Homo sapiens]

Protein Classification

C2-C2_1 and C2 domain-containing protein (domain architecture ID 11767164)

protein containing domains SMC_N, C2-C2_1, and C2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
619-756 2.04e-63

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


:

Pssm-ID: 314488  Cd Length: 140  Bit Score: 214.05  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   619 SLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEAS 698
Cdd:pfam11618    1 VELERGENLFELHIGGATFSPEALRELGDKEPATFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLHYLQTGS 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   699 ARLDIHQAMASEHSTLAAGWICFDRVLETVEKVHGLATLIGAGGEE--FGVLEYWMRLRF 756
Cdd:pfam11618   81 LTLELHQALGVDFKTLAAAQLRLHGLLEKNGKVIGSVSLVGVEGEIqaFGTLEYWIRLRV 140
SMC_N super family cl25732
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
258-582 7.81e-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.


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 330553  Cd Length: 1179  Bit Score: 60.07  E-value: 7.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   258 ECAQKAAELRASIKEkVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLlqknqgilSAAHEALLKQVNELRAELKEes 337
Cdd:TIGR02168  210 EKAERYKELKAELRE-LELALLVLRLEELREELEELQEELKEAEEELEEL--------TAELQELEEKLEELRLEVSE-- 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   338 kkavsLKSQLEDvsiLQMTLKEFQERVEDLEKERKLLNDNYDKLLESmldssdsssqphwsneliaeqlqqqVSQLQDQL 417
Cdd:TIGR02168  279 -----LEEEIEE---LQKELYALANEISRLEQQKQILRERLANLERQ-------------------------LEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   418 DAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQPPDRQSEPathpavlQENTQIEPSEPKNQE 497
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-------LRSKVAQLELQIASL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   498 EKKLSQV---LNELQVSHAETTLELEKTRDMLILQRKINVCYQ-EELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIK 573
Cdd:TIGR02168  399 NNEIERLearLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                   ....*....
gi 112734867   574 QLEGILRSH 582
Cdd:TIGR02168  479 AAERELAQL 487
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
801-908 2.30e-08

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175973  Cd Length: 102  Bit Score: 54.77  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  801 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 880
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|....*....
gi 112734867  881 EPGSYLGRARVPLLPLA-KNESIKGDFNL 908
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
 
Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
619-756 2.04e-63

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 314488  Cd Length: 140  Bit Score: 214.05  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   619 SLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEAS 698
Cdd:pfam11618    1 VELERGENLFELHIGGATFSPEALRELGDKEPATFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLHYLQTGS 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   699 ARLDIHQAMASEHSTLAAGWICFDRVLETVEKVHGLATLIGAGGEE--FGVLEYWMRLRF 756
Cdd:pfam11618   81 LTLELHQALGVDFKTLAAAQLRLHGLLEKNGKVIGSVSLVGVEGEIqaFGTLEYWIRLRV 140
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-582 7.81e-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  Cd Length: 1179  Bit Score: 60.07  E-value: 7.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   258 ECAQKAAELRASIKEkVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLlqknqgilSAAHEALLKQVNELRAELKEes 337
Cdd:TIGR02168  210 EKAERYKELKAELRE-LELALLVLRLEELREELEELQEELKEAEEELEEL--------TAELQELEEKLEELRLEVSE-- 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   338 kkavsLKSQLEDvsiLQMTLKEFQERVEDLEKERKLLNDNYDKLLESmldssdsssqphwsneliaeqlqqqVSQLQDQL 417
Cdd:TIGR02168  279 -----LEEEIEE---LQKELYALANEISRLEQQKQILRERLANLERQ-------------------------LEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   418 DAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQPPDRQSEPathpavlQENTQIEPSEPKNQE 497
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-------LRSKVAQLELQIASL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   498 EKKLSQV---LNELQVSHAETTLELEKTRDMLILQRKINVCYQ-EELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIK 573
Cdd:TIGR02168  399 NNEIERLearLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                   ....*....
gi 112734867   574 QLEGILRSH 582
Cdd:TIGR02168  479 AAERELAQL 487
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
801-908 2.30e-08

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973  Cd Length: 102  Bit Score: 54.77  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  801 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 880
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|....*....
gi 112734867  881 EPGSYLGRARVPLLPLA-KNESIKGDFNL 908
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
249-581 1.22e-07

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


Pssm-ID: 223496  Cd Length: 908  Bit Score: 56.31  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  249 ENFEQRSSLECAQKA--AELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHEALLKQV 326
Cdd:COG0419   305 EELEGLRALLEELEEllEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  327 NELRAELKEESKKAVSLKSQLEDVsilQMTLKEFQERVEDLEKERKLLNDNYdKLLESMLDSSDSSSQPHWSNELIAEQL 406
Cdd:COG0419   385 KQLEEAIQELKEELAELSAALEEI---QEELEELEKELEELERELEELEEEI-KKLEEQINQLESKELMIAELAGAGEKC 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  407 QQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISqppdrqsepathpavLQENT 486
Cdd:COG0419   461 PVCGQELPEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIEL---------------LELEE 525
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  487 QIEPSepKNQEEKKLSQVLNELQVSHAETTLE--LEKTRDMLILQRKINvcyqEELEAMmtkadNDNRDHKEKLERLTRL 564
Cdd:COG0419   526 ALKEE--LEEKLEKLENLLEELEELKEKLQLQqlKEELRQLEDRLQELK----ELLEEL-----RLLRTRKEELEELRER 594
                         330
                  ....*....|....*..
gi 112734867  565 LDLKNNRIKQLEGILRS 581
Cdd:COG0419   595 LKELKKKLKELEERLSQ 611
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
227-571 1.35e-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  Cd Length: 787  Bit Score: 49.33  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   227 MASNTMQVEEPPKSPEKMWPKDENFEQRSSLECAQKAAELRASIK----EKVELIRLKKLLHERNaSLVMTKAQLTEVQE 302
Cdd:pfam05483  354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELEELKKILAEDE-KLLDEKKQFEKIAE 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   303 AYETLLQKNQGILSA-----------------AHEALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTL-KEFQERV 364
Cdd:pfam05483  433 ELKGKEQELIFLLQArekeihdleiqltaiktSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtQEASDMT 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   365 EDLEKERKLLNDNY---DKLLESMLDSSDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDL 441
Cdd:pfam05483  513 LELKKHQEDIINCKkqeERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   442 KLEVTN----ILQKHKQEVELLQNAATISQPPDRQSEPATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQ---VSHAE 514
Cdd:pfam05483  593 ENKCNNlkkqIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkISEEK 672
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112734867   515 TTLELEKTR----DMLILQRKINVCYQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNR 571
Cdd:pfam05483  673 LLEEVEKAKaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
C2 pfam00168
C2 domain;
803-908 1.43e-04

C2 domain;


Pssm-ID: 306639  Cd Length: 104  Bit Score: 43.07  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   803 IEITKCCGLRSRWLGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDE 878
Cdd:pfam00168    5 VTVIEAKNLPPKDLNGKSDPYVK---VYLLDGKqkkkTKVVKNTLNPVWNETFTFSV-------PDPENAVLEIEVYDYD 74
                           90       100       110
                   ....*....|....*....|....*....|
gi 112734867   879 DLEPGSYLGRARVPLLPLAKNESIKGDFNL 908
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEVLDGWYPL 104
PTZ00121 PTZ00121
MAEBL; Provisional
233-551 8.75e-04

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 43.59  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  233 QVEEPPKSPEKmwpKDENFEQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQ 312
Cdd:PTZ00121 1582 KAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  313 GILSAAHEAL-----LKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLD 387
Cdd:PTZ00121 1659 NKIKAAEEAKkaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  388 SSDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQ 467
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  468 PPDRQSE----PATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLilqrkinvcyQEELEAM 543
Cdd:PTZ00121 1819 LVINDSKemedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE----------EEIEEAD 1888

                  ....*...
gi 112734867  544 MTKADNDN 551
Cdd:PTZ00121 1889 EIEKIDKD 1896
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
803-904 3.50e-03

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577  Cd Length: 101  Bit Score: 38.62  E-value: 3.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867    803 IEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHD--TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDEDL 880
Cdd:smart00239    4 VKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEV-------PPPELAELEIEVYDKDRF 76
                            90       100
                    ....*....|....*....|....
gi 112734867    881 EPGSYLGRARVPLLPLAKNESIKG 904
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEK 100
 
Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
619-756 2.04e-63

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 314488  Cd Length: 140  Bit Score: 214.05  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   619 SLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEAS 698
Cdd:pfam11618    1 VELERGENLFELHIGGATFSPEALRELGDKEPATFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLHYLQTGS 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   699 ARLDIHQAMASEHSTLAAGWICFDRVLETVEKVHGLATLIGAGGEE--FGVLEYWMRLRF 756
Cdd:pfam11618   81 LTLELHQALGVDFKTLAAAQLRLHGLLEKNGKVIGSVSLVGVEGEIqaFGTLEYWIRLRV 140
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-582 7.81e-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  Cd Length: 1179  Bit Score: 60.07  E-value: 7.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   258 ECAQKAAELRASIKEkVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLlqknqgilSAAHEALLKQVNELRAELKEes 337
Cdd:TIGR02168  210 EKAERYKELKAELRE-LELALLVLRLEELREELEELQEELKEAEEELEEL--------TAELQELEEKLEELRLEVSE-- 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   338 kkavsLKSQLEDvsiLQMTLKEFQERVEDLEKERKLLNDNYDKLLESmldssdsssqphwsneliaeqlqqqVSQLQDQL 417
Cdd:TIGR02168  279 -----LEEEIEE---LQKELYALANEISRLEQQKQILRERLANLERQ-------------------------LEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   418 DAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQPPDRQSEPathpavlQENTQIEPSEPKNQE 497
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-------LRSKVAQLELQIASL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   498 EKKLSQV---LNELQVSHAETTLELEKTRDMLILQRKINVCYQ-EELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIK 573
Cdd:TIGR02168  399 NNEIERLearLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                   ....*....
gi 112734867   574 QLEGILRSH 582
Cdd:TIGR02168  479 AAERELAQL 487
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
801-908 2.30e-08

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973  Cd Length: 102  Bit Score: 54.77  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  801 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 880
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|....*....
gi 112734867  881 EPGSYLGRARVPLLPLA-KNESIKGDFNL 908
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
249-581 1.22e-07

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


Pssm-ID: 223496  Cd Length: 908  Bit Score: 56.31  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  249 ENFEQRSSLECAQKA--AELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHEALLKQV 326
Cdd:COG0419   305 EELEGLRALLEELEEllEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  327 NELRAELKEESKKAVSLKSQLEDVsilQMTLKEFQERVEDLEKERKLLNDNYdKLLESMLDSSDSSSQPHWSNELIAEQL 406
Cdd:COG0419   385 KQLEEAIQELKEELAELSAALEEI---QEELEELEKELEELERELEELEEEI-KKLEEQINQLESKELMIAELAGAGEKC 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  407 QQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISqppdrqsepathpavLQENT 486
Cdd:COG0419   461 PVCGQELPEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIEL---------------LELEE 525
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  487 QIEPSepKNQEEKKLSQVLNELQVSHAETTLE--LEKTRDMLILQRKINvcyqEELEAMmtkadNDNRDHKEKLERLTRL 564
Cdd:COG0419   526 ALKEE--LEEKLEKLENLLEELEELKEKLQLQqlKEELRQLEDRLQELK----ELLEEL-----RLLRTRKEELEELRER 594
                         330
                  ....*....|....*..
gi 112734867  565 LDLKNNRIKQLEGILRS 581
Cdd:COG0419   595 LKELKKKLKELEERLSQ 611
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-575 1.32e-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  Cd Length: 1179  Bit Score: 56.22  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   261 QKAAELRASIKEKVELIR-LKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGI------LSAAHEALLKQVNELRAEL 333
Cdd:TIGR02168  698 KALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelteLEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   334 KEESKKAVSLKSQLEDVSILqmtLKEFQERVEDLEKERKLLNDNYDKLLESMLDSSDSSSQPHWSNELIAEqlqqqvsql 413
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--------- 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   414 qdqldaELEDKRKVLLELSREKAQNEDLklevtniLQKHKQEVELLQNAAtisqppdRQSEPATHPAVLQENTQIEPSEP 493
Cdd:TIGR02168  846 ------QIEELSEDIESLAAEIEELEEL-------IEELESELEALLNER-------ASLEEALALLRSELEELSEELRE 905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   494 KNQEEKKLSQVLNELQVSHAETTLELEKTRDMLI-LQRKINVCYQEELEAMMTKADNDNRDHKEKLERLTRLldlkNNRI 572
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKI 981

                   ...
gi 112734867   573 KQL 575
Cdd:TIGR02168  982 KEL 984
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
816-934 5.15e-06

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019  Cd Length: 127  Bit Score: 47.63  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  816 LGTQPSPYAVYRFFTFSdHDTAIIPASNNPYFRDQARFPVlvTSDLDhylRREALSIHVFDDEDLEPGSYLGRARVPLLP 895
Cdd:cd08373    11 LKGKGDRIAKVTFRGVK-KKTRVLENELNPVWNETFEWPL--AGSPD---PDESLEIVVKDYEKVGRNRLIGSATVSLQD 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 112734867  896 LAKNESIKGDFNLTDPAEKPNG-SIQVQLDwkfpYIPPES 934
Cdd:cd08373    85 LVSEGLLEVTEPLLDSNGRPTGaTISLEVS----YQPPDG 120
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
247-523 5.65e-06

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 50.87  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  247 KDENFEQRSSLEcAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQgILSAAHEALLKQV 326
Cdd:COG1196   241 LEELEEELSRLE-EELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS-LLRERLEELENEL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  327 NELRAELKEESKKAVSLKSQLE----DVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESmldssdsssqphWSNELI 402
Cdd:COG1196   319 EELEERLEELKEKIEALKEELEeretLLEELEQLLAELEEAKEELEEKLSALLEELEELFEA------------LREELA 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  403 AEqlqqqvsqlqdqlDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLqnaatisqppdRQSEPATHPAVL 482
Cdd:COG1196   387 EL-------------EAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKEL-----------EAELEELQTELE 442
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 112734867  483 QENTQIEPSEPKNQEEK----KLSQVLNELQVSHAETTLELEKTR 523
Cdd:COG1196   443 ELNEELEELEEQLEELRdrlkELERELAELQEELQRLEKELSSLE 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
296-576 7.39e-06

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  Cd Length: 1179  Bit Score: 50.44  E-value: 7.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   296 QLTEVQEAYETLLQKNQGILSAAHEALLKQVNELRAELKEESKKAVSLKSQLEdvsILQMTLKEFQERVEDLEKERKLLN 375
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA---RLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   376 DNYDKLLEsmldssdsssQPHWSNELIAEqlqqqvsqlqdqLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQE 455
Cdd:TIGR02168  761 AEIEELEE----------RLEEAEEELAE------------AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   456 VELLQNAATISQppDRQSEPATHPAVLQENTqiepsEPKNQEEKKLSQVLNELQVSHAETTLELEKtrdMLILQRKINVc 535
Cdd:TIGR02168  819 AANLRERLESLE--RRIAATERRLEDLEEQI-----EELSEDIESLAAEIEELEELIEELESELEA---LLNERASLEE- 887
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 112734867   536 YQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIKQLE 576
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
227-571 1.35e-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  Cd Length: 787  Bit Score: 49.33  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   227 MASNTMQVEEPPKSPEKMWPKDENFEQRSSLECAQKAAELRASIK----EKVELIRLKKLLHERNaSLVMTKAQLTEVQE 302
Cdd:pfam05483  354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELEELKKILAEDE-KLLDEKKQFEKIAE 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   303 AYETLLQKNQGILSA-----------------AHEALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTL-KEFQERV 364
Cdd:pfam05483  433 ELKGKEQELIFLLQArekeihdleiqltaiktSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtQEASDMT 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   365 EDLEKERKLLNDNY---DKLLESMLDSSDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDL 441
Cdd:pfam05483  513 LELKKHQEDIINCKkqeERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   442 KLEVTN----ILQKHKQEVELLQNAATISQPPDRQSEPATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQ---VSHAE 514
Cdd:pfam05483  593 ENKCNNlkkqIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkISEEK 672
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112734867   515 TTLELEKTR----DMLILQRKINVCYQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNR 571
Cdd:pfam05483  673 LLEEVEKAKaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
252-584 1.97e-05

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


Pssm-ID: 223496  Cd Length: 908  Bit Score: 48.99  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  252 EQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHE----------- 320
Cdd:COG0419   220 EIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEkierleelere 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  321 ------------ALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLDS 388
Cdd:COG0419   300 ieeleeeleglrALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEK 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  389 SDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDlklEVTNILQKHKQEVELLQNAATISQP 468
Cdd:COG0419   380 ALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEE---EIKKLEEQINQLESKELMIAELAGA 456
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  469 PDR-----QSEPATHPAVLQE--NTQIEPSEPKNQEEKKLSQVLNELQvshaETTLELEKTRDMLILQRKINVCYQEELE 541
Cdd:COG0419   457 GEKcpvcgQELPEEHEKELLElyELELEELEEELSREKEEAELREEIE----ELEKELRELEEELIELLELEEALKEELE 532
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 112734867  542 AMMTKADN-----DNRDHKEKLERLTRLLDLKNNRIKQLEGILRSHDL 584
Cdd:COG0419   533 EKLEKLENlleelEELKEKLQLQQLKEELRQLEDRLQELKELLEELRL 580
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
262-576 2.33e-05

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


Pssm-ID: 223496  Cd Length: 908  Bit Score: 48.60  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  262 KAAELRASIKEKVELIRLKKLLHERNasLVMTKAQLTEVQEAYETLLQKNQGILSAAHEALLKQVNELRAELKEESKKAV 341
Cdd:COG0419   179 VIKEAKAKIEELEGQLSELLEDIEDL--LEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKA 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  342 SLKS----QLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLEsmldssdsssqphwSNELIAEQLQQQVSQLQDQL 417
Cdd:COG0419   257 RLLEieslELEALKIREEELRELERLLEELEEKIERLEELEREIEE--------------LEEELEGLRALLEELEELLE 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  418 DAELEDKRKVLLELSREKAQNEDLKLEVTNILQK---HKQEVELLQNAATISQPPDRQSEPAThpaVLQENTQIEPSEPK 494
Cdd:COG0419   323 KLKSLEERLEKLEEKLEKLESELEELAEEKNELAkllEERLKELEERLEELEKELEKALERLK---QLEEAIQELKEELA 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  495 NQEEK--KLSQVLNELQVSHAETTLELEK-TRDMLILQRKINVCYQEELEAMMTKADND-----NRDHKEKLERltRLLD 566
Cdd:COG0419   400 ELSAAleEIQEELEELEKELEELERELEElEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcGQELPEEHEK--ELLE 477
                         330
                  ....*....|
gi 112734867  567 LKNNRIKQLE 576
Cdd:COG0419   478 LYELELEELE 487
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
278-576 2.34e-05

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 48.56  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  278 RLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQgILSAAHEALLKQVNELRAELKEESKKAVSLKSQLEdvsilqmtl 357
Cdd:COG1196   657 RNKRSSLAQKRELKELEEELAELEAQLEKLEEELK-SLKNELRSLEDLLEELRRQLEELERQLEELKRELA--------- 726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  358 kEFQERVEDLEKERKLLNDNYDKLLESMldssdsssqphwsneliaeqlqqqvsqlqDQLDAELEDKRKVLLELSREKAQ 437
Cdd:COG1196   727 -ALEEELEQLQSRLEELEEELEELEEEL-----------------------------EELQERLEELEEELESLEEALAK 776
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  438 NEDLKLEVTNILQKHKQEVELLQNAAtisqppdRQSEPATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTL 517
Cdd:COG1196   777 LKEEIEELEEKRQALQEELEELEEEL-------EEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEE 849
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 112734867  518 ELEKTRDmlilQRKINVCYQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIKQLE 576
Cdd:COG1196   850 ELEELEK----ELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELK 904
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
304-594 2.63e-05

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 48.56  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  304 YETLLQKNQGILSAAhEALLKQVNELRAEL----------KEESKKAVSLKSQLEDV--SILQMTLKEFQERVEDLEKER 371
Cdd:COG1196   170 YKERKEEAERKLERT-EENLERLEDLLEELekqleklerqAEKAERYQELKAELRELelALLLAKLKELRKELEELEEEL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  372 KLLNDNYDKLLESMldssdsssqphwsneliaeqlqqqvsqlqDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQK 451
Cdd:COG1196   249 SRLEEELEELQEEL-----------------------------EEAEKEIEELKSELEELREELEELQEELLELKEEIEE 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  452 HKQEVELLQNAATISQppDRQSEPATHPAVLQEntQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLI--LQ 529
Cdd:COG1196   300 LEGEISLLRERLEELE--NELEELEERLEELKE--KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLeeLE 375
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112734867  530 RKINVC--YQEELEAMMTKADNDNRDHKEKLERLTRLLDLKNNRIKQLEGILRSHDLPTSEQLKDVA 594
Cdd:COG1196   376 ELFEALreELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
248-576 2.65e-05

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


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 48.53  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   248 DENFEQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNA---SLVMTKAQL---TEVQEAYETLLQKNQGILSAAhEA 321
Cdd:TIGR02169  194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEAlerQKEAIERQLaslEEELEKLTEEISELEKRLEEI-EQ 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   322 LLKQVNELRAELKEEskKAVSLKSQLEDVSI----LQMTLKEFQERVEDLEKERKLLNDNYDKLLESMldssdsssqphw 397
Cdd:TIGR02169  273 LLEELNKKIKDLGEE--EQLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEI------------ 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   398 sNELiaEQLQQQVSQLQDQLDAELEDKRKVLlELSREKAQNEDLKLEVTniLQKHKQEVEllqnaaTISQPPDRQSEPAT 477
Cdd:TIGR02169  339 -EEL--EREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAET--RDELKDYRE------KLEKLKREINELKR 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   478 HPAVLQENTQ---IEPSEPKNQEEKKLSQvLNELQVSHAETTLELEKTRDMLilqrkinvcyqEELEAMMTKADNDNRDH 554
Cdd:TIGR02169  407 ELDRLQEELQrlsEELADLNAAIAGIEAK-INELEEEKEDKALEIKKQEWKL-----------EQLAADLSKYEQELYDL 474
                          330       340
                   ....*....|....*....|..
gi 112734867   555 KEKLERLTRLLDLKNNRIKQLE 576
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAEAE 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
247-461 4.11e-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  Cd Length: 1179  Bit Score: 48.13  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   247 KDENFEQRSSLECAQKA--------AELRASIKE-KVELIRLKKLLHERNASLVMTKAQLTEVQEAyETLLQKNQGILSA 317
Cdd:TIGR02168  273 RLEVSELEEEIEELQKElyalaneiSRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEE-LAELEEKLEELKE 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   318 AHEALLKQVNELRAELKEESKKAVSLKSQLE----DVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESmLDSSDSSS 393
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKL 430
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112734867   394 QPHWSNELIAEQLQQQVSQLQDqlDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQN 461
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
253-581 7.20e-05

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 47.02  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  253 QRSSLECAQKAAELRASIKEKVELIR-LKKLLHERNASLVMTKAQLTEVQEAYE------TLLQKNQGILSAAHEALLKQ 325
Cdd:COG1196   680 EAQLEKLEEELKSLKNELRSLEDLLEeLRRQLEELERQLEELKRELAALEEELEqlqsrlEELEEELEELEEELEELQER 759
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  326 VNELRAELKEESKKAVSLKSQLEDVSILqmtLKEFQERVEDLEKERKLLNDNYDKLLESMLdssdsssqphwSNELIAEQ 405
Cdd:COG1196   760 LEELEEELESLEEALAKLKEEIEELEEK---RQALQEELEELEEELEEAERRLDALERELE-----------SLEQRRER 825
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  406 LQQQVSQLQDQLDaELEDKRKVL-LELSREKAQNEDLKLEVTNiLQKHKQEVE-LLQNAATISQPPDRQSEPATHPAVLQ 483
Cdd:COG1196   826 LEQEIEELEEEIE-ELEEKLDELeEELEELEKELEELKEELEE-LEAEKEELEdELKELEEEKEELEEELRELESELAEL 903
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  484 ENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLIlQRKINVCyQEELEAMMtkadNDNRDHKEKLERLTR 563
Cdd:COG1196   904 KEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETEL-EREIERL-EEEIEALG----PVNLRAIEEYEEVEE 977
                         330
                  ....*....|....*...
gi 112734867  564 LLDLKNNRIKQLEGILRS 581
Cdd:COG1196   978 RYEELKSQREDLEEAKEK 995
HOOK pfam05622
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ...
247-576 7.43e-05

HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas the central coiled-coil motif mediates homodimerisation and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head.


Pssm-ID: 310310  Cd Length: 701  Bit Score: 46.98  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   247 KDENFEQRsslECAQKAAELRASI---KEKVE----LIRLKKLLHERNASLVMTKAQLTEvqEAYETLLQKNQgilsaaH 319
Cdd:pfam05622  291 KDEIDILR---ESSDKVSKLEATVetyKKKLEdlndLRRQVKLLEERNAVYMQNTVELEE--ELRKANALRGQ------L 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   320 EALLKQVNELRAELKEESKKAVSLksqledvsilQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLDSSDSSSQPHwsN 399
Cdd:pfam05622  360 ETYKRQVQELHGKLSEESKKADKL----------EFEYKKLEEKLEALQKEKERLIIERDSLRETNEELRCAQLQQD--E 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   400 ELIAEQLQQQVSQLQDQLDAEL--EDKRKVLLELSRE--------KAQNEDLKLEVTNILQKHKQEVELLQNAATISQpp 469
Cdd:pfam05622  428 LSQADNLLSPSSDSGDNLAAELmpPEVREKLIRLQHEnkmlrlqqEGSEREKLTELQALLEDANRRLNELRTQNRLAN-- 505
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   470 DRQSEPATHPAVLQENTQIEPSepKNQEEKKLSQVLNELQVSHAETTLELEKTRDML-ILQRKINVCYQ--EELEAMMTK 546
Cdd:pfam05622  506 QRILELQAQVEELQKALQEQGS--KAEDSSLLKKKLEEHLEKLHEAQSELQKKKEQLeELEPDLNSNKQkiDELQAALKK 583
                          330       340       350
                   ....*....|....*....|....*....|
gi 112734867   547 ADNDNRDHKeklERLTRLLDLKNNRIKQLE 576
Cdd:pfam05622  584 KDEDMKAME---ERYKKYVEKAKSVIKTLD 610
C2 pfam00168
C2 domain;
803-908 1.43e-04

C2 domain;


Pssm-ID: 306639  Cd Length: 104  Bit Score: 43.07  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   803 IEITKCCGLRSRWLGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDE 878
Cdd:pfam00168    5 VTVIEAKNLPPKDLNGKSDPYVK---VYLLDGKqkkkTKVVKNTLNPVWNETFTFSV-------PDPENAVLEIEVYDYD 74
                           90       100       110
                   ....*....|....*....|....*....|
gi 112734867   879 DLEPGSYLGRARVPLLPLAKNESIKGDFNL 908
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEVLDGWYPL 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
262-581 3.02e-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  Cd Length: 1164  Bit Score: 45.06  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   262 KAAELRASIKE--------KVELIRLKKLLHERNASLVMTKAQLTEvqeayetlLQKNQGILSAAHEALLKQVNELRAEL 333
Cdd:TIGR02169  675 ELQRLRERLEGlkrelsslQSELRRIENRLDELSQELSDASRKIGE--------IEKEIEQLEQEEEKLKERLEELEEDL 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   334 KEESKKAVSLKSQLEDVSilqmtlKEFQERVEDLEKERKLLNDNYDKLLESMLDSSDSSSQphwsneliaeqlqqqvsql 413
Cdd:TIGR02169  747 SSLEQEIENVKSELKELE------ARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS------------------- 801
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   414 qdQLDAELEDKRKVLLELSReKAQNEDLKLEvtnILQKHKQEVELLQNAATIsQPPDRQSEpathpavlQENTQIEPSEp 493
Cdd:TIGR02169  802 --KLEEEVSRIEARLREIEQ-KLNRLTLEKE---YLEKEIQELQEQRIDLKE-QIKSIEKE--------IENLNGKKEE- 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   494 KNQEEKKLSQVLNELQVSHAettlELEKTRDMLI-----LQRKINvcyqeELEAMMTKAdndnrdhKEKLERLTRLLDLK 568
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLG----DLKKERDELEaqlreLERKIE-----ELEAQIEKK-------RKRLSELKAKLEAL 929
                          330
                   ....*....|...
gi 112734867   569 NNRIKQLEGILRS 581
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
816-928 7.43e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009  Cd Length: 124  Bit Score: 40.62  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  816 LGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQarFPVLVTSDLDHylrreaLSIHVFDDEDLEPGSYLGRARV 891
Cdd:cd04044    20 IGGTVDPYVT---FSISNRRelarTKVKKDTSNPVWNET--KYILVNSLTEP------LNLTVYDFNDKRKDKLIGTAEF 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 112734867  892 PLLPLAKNESIKgdfNLTDP---AEKPNGSIQVQLDWkFP 928
Cdd:cd04044    89 DLSSLLQNPEQE---NLTKNllrNGKPVGELNYDLRF-FP 124
APG6 pfam04111
Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
257-381 8.01e-04

Autophagy protein Apg6; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 309295  Cd Length: 308  Bit Score: 42.94  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   257 LECAQKA-----AELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEayetlLQKNQGILSAAHEALLKQVNELRA 331
Cdd:pfam04111    4 EECTDLLleeldKELEQLEKERDAYQEFLKKLEKEKPSDEEIEALEKELEK-----LEKEEEELLQELEELEKEREELDA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 112734867   332 ELKEESKKAVSLKSQ----LEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKL 381
Cdd:pfam04111   79 ELEKLEEELEELDEEeeeyWREYNAFQLELLEFQDERDSLENQYEHAQDQLDRL 132
PTZ00121 PTZ00121
MAEBL; Provisional
233-551 8.75e-04

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 43.59  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  233 QVEEPPKSPEKmwpKDENFEQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQ 312
Cdd:PTZ00121 1582 KAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  313 GILSAAHEAL-----LKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLD 387
Cdd:PTZ00121 1659 NKIKAAEEAKkaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  388 SSDSSSQPHWSNELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQ 467
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  468 PPDRQSE----PATHPAVLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLilqrkinvcyQEELEAM 543
Cdd:PTZ00121 1819 LVINDSKemedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE----------EEIEEAD 1888

                  ....*...
gi 112734867  544 MTKADNDN 551
Cdd:PTZ00121 1889 EIEKIDKD 1896
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
249-577 9.17e-04

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


Pssm-ID: 129705  Cd Length: 1042  Bit Score: 43.42  E-value: 9.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   249 ENFEQRSSLECAQKAAELRASIkEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHEALLKQ--V 326
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSQL-LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQqlL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   327 NELRAELKE--ESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYdKLLESMLDSSDSSSQPHWSNEliae 404
Cdd:TIGR00618  263 KQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLMKRAAHVKQQ---- 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   405 qlqqqvsqlqdqldAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQ--PPDRQSEPATHPAVL 482
Cdd:TIGR00618  338 --------------SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkTTLTQKLQSLCKELD 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   483 QENTQIEPSEPKNQEEKKLSQvlnelQVSHAETTLELEKtRDMLILQRKINVCYQEEL--EAMMTKADNDNRDHKEKLER 560
Cdd:TIGR00618  404 ILQREQATIDTRTSAFRDLQG-----QLAHAKKQQELQQ-RYAELCAAAITCTAQCEKleKIHLQESAQSLKEREQQLQT 477
                          330
                   ....*....|....*..
gi 112734867   561 LTRLLdLKNNRIKQLEG 577
Cdd:TIGR00618  478 KEQIH-LQETRKKAVVL 493
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
273-376 1.05e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerisation of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 311742  Cd Length: 124  Bit Score: 40.28  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   273 KVELIRLKKLLHERNASLVMTKAQL-------TEVQEAYETLLQKnqgilsaaHEALLKQVNELRAELKEESKKAVSLKS 345
Cdd:pfam07926    2 ESEIKRLKEEIEEYEAQLQSLQEDLesqaeiaKEAQQKYERELVL--------HAEDIKALQALREELNELKQEIAELKA 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 112734867   346 QLEDV---------------SILQMTLKEFQERVEDLEKERKLLND 376
Cdd:pfam07926   74 EAESAkaeleeseesweeqkKELEKELSELEKRIEDLNEQNKLLHD 119
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
252-577 1.16e-03

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


Pssm-ID: 223496  Cd Length: 908  Bit Score: 43.21  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  252 EQRSSLEcaQKAAELRASIKE-KVELIRLKKLLHERNASLVMTKAQL---TEVQEAYETLLQKNQGILSAAHEALLKQVN 327
Cdd:COG0419   329 ERLEKLE--EKLEKLESELEElAEEKNELAKLLEERLKELEERLEELekeLEKALERLKQLEEAIQELKEELAELSAALE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  328 ELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDK---LLESMLDSSDSSSQPHWSNELIAE 404
Cdd:COG0419   407 EIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKcpvCGQELPEEHEKELLELYELELEEL 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  405 QLQQQVSQLQDQLDAELEDKRKVLLELSREKAQ----NEDLKLEVTNILQKHKQEVELLQNAATISQPPDRQSEPATHPA 480
Cdd:COG0419   487 EEELSREKEEAELREEIEELEKELRELEEELIEllelEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLED 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  481 VLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTrdMLILQRKINVCYQEELEAMMTKADNDNRDHKEKLER 560
Cdd:COG0419   567 RLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEER--LSQLEELLQSLELSEAENELEEAEEELESELEKLNL 644
                         330
                  ....*....|....*..
gi 112734867  561 LTRLLDLKNNRIKQLEG 577
Cdd:COG0419   645 QAELEELLQAALEELEE 661
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
241-467 1.26e-03

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


Pssm-ID: 129705  Cd Length: 1042  Bit Score: 43.03  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   241 PEKMWPKDENFEQRsslecAQKAAELRASIKEKVELIRLkkLLHERNASLVMTKAQLTEVQEAYETLLQKNQGILSAAHE 320
Cdd:TIGR00618  671 PKELLASRQLALQK-----MQSEKEQLTYWKEMLAQCQT--LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   321 ALlkqvNELRAELKEESKKAVSLKSQ-LEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLEsmLDSSDSSSQPHwsN 399
Cdd:TIGR00618  744 SL----KELMHQARTVLKARTEAHFNnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT--LEAEIGQEIPS--D 815
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112734867   400 ELIAEQLQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQ 467
Cdd:TIGR00618  816 EDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQ 883
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
321-382 1.55e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461  Cd Length: 425  Bit Score: 42.36  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112734867  321 ALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLL 382
Cdd:PRK05431   39 ELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEELL 100
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
252-552 2.12e-03

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


Pssm-ID: 224117  Cd Length: 1163  Bit Score: 42.39  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  252 EQRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLvmtKAQLTEVQEAYETL------LQKNQGILSAAHEALLKQ 325
Cdd:COG1196   220 AELRELELALLLAKLKELRKELEELEEELSRLEEELEEL---QEELEEAEKEIEELkseleeLREELEELQEELLELKEE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  326 VNELRAELKEESKKAVSLKSQLEDvsiLQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLdssdsssqphwSNELIAEQ 405
Cdd:COG1196   297 IEELEGEISLLRERLEELENELEE---LEERLEELKEKIEALKEELEERETLLEELEQLLA-----------ELEEAKEE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867  406 LQQQVSQLQDQLDAELEDKRKVLLELSREKAQNEdlklevtNILQKHKQEVELLQNAATISQPPDRQSEPATHPAVLQEN 485
Cdd:COG1196   363 LEEKLSALLEELEELFEALREELAELEAELAEIR-------NELEELKREIESLEERLERLSERLEDLKEELKELEAELE 435
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112734867  486 TQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLILQRKINVCYQEELEAMMTKADNDNR 552
Cdd:COG1196   436 ELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
803-904 3.50e-03

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577  Cd Length: 101  Bit Score: 38.62  E-value: 3.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867    803 IEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHD--TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDEDL 880
Cdd:smart00239    4 VKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEV-------PPPELAELEIEVYDKDRF 76
                            90       100
                    ....*....|....*....|....
gi 112734867    881 EPGSYLGRARVPLLPLAKNESIKG 904
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEK 100
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
133-444 3.78e-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: 313027  Cd Length: 597  Bit Score: 41.26  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   133 PASPRRAQPRVQVgHRQLHTAGAPVPEKPKRGP----RDRLSYTAPPSFKEHATNENRGEVASKPSELVSGSNSIISFSS 208
Cdd:pfam09731  107 EATKDEAEAKAQQ-PKSEQEKEKALEEVLKEAIskaeSVTAVAKEAKDDARNAVDEAVDSLKEASETTKINRESARDKQS 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   209 VISMAKPIGLCMPNSAHIMASNTMQVEEPPKSPEKMWPKDENFEQRSSLECAQKAAELrASIkekveLIRLKKLLHERNA 288
Cdd:pfam09731  186 EITSLPPLLDAAPETPPKLTEHLDKVVETVEKARSLASLVEKYKELVASERIVFQQEL-VSI-----FPDIIPVLKEDNI 259
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   289 SLVMTKAQLTeVQEAYETLLQKNQGILSAAHEALLKQVNELRAELKEESKKAVSLKSQLEDVsilqMTLKEFQERVEdLE 368
Cdd:pfam09731  260 KLSNDDLNSL-IAHAHEEIDALSKKLAELKAEEEKHIERALKKKKEELDKQAEALSARLEEV----RAKDEKQLRLE-FE 333
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112734867   369 KERKLLNDNYDKLLESMLDSSDSSSQPHWSNELIAeqlqqqvsqlqdqldAELEDKRKVLLELSREKAQNEDLKLE 444
Cdd:pfam09731  334 REIEEIRESYEEKLRTELERQAEAHEEHLKDVLVE---------------QEIELKREFLQDIKEKVEKERAGRLL 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
253-461 4.23e-03

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


Pssm-ID: 274008  Cd Length: 1179  Bit Score: 41.20  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   253 QRSSLECAQKAAELRASIKEKVELIRLKKLLHERNASLVMTKAQLTEVQEAYETLLQKnqgiLSAAHEALLKQVNELRAE 332
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   333 LKEESKKAVSLKSQLE----DVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMLDSSDSSSqpHWSNELIAEQLQQ 408
Cdd:TIGR02168  812 LTLLNEEAANLRERLEslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEAL 889
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 112734867   409 QVSQLqdqldaELEDKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQN 461
Cdd:TIGR02168  890 ALLRS------ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
279-630 5.33e-03

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


Pssm-ID: 318193  Cd Length: 1112  Bit Score: 40.87  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   279 LKKLLHERNASLVMTKAQLTEVQEAYETLLQKNQG---ILSAAHEALLKQ-VNELRAELKEESKKAVSLKSQLEDV---- 350
Cdd:pfam15921  222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkieLLLQQHQDRIEQlISEHEVEITGLTEKASSARSQANSIqsql 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   351 -----------SILQMTLKEFQERVEDLEKERKLLNDNYDKLLESMldssdsSSQPHWSNELIAEQLQQQVSQLQDqlDA 419
Cdd:pfam15921  302 eiiqeqarnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL------EKQLVLANSELTEARTERDQFSQE--SG 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   420 ELEDKRKVLL--------ELSREKAQNEDLKLEVTNilqkhkqevellqNAATIS----QPPDRQSEPATHPAVLQENTq 487
Cdd:pfam15921  374 NLDDQLQKLLadlhkrekELSLEKEQNKRLWDRDTG-------------NSITIDhlrrELDDRNMEVQRLEALLKAMK- 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   488 iepSEPKNQEEKKLS--QVLNELQVSHAETTLELEKTRDMLilqRKInvcyQEELEAMMTKADNDNR---DHKEKLERLT 562
Cdd:pfam15921  440 ---SECQGQMERQMAaiQGKNESLEKVSSLTAQLESTKEML---RKV----VEELTAKKMTLESSERtvsDLTASLQEKE 509
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112734867   563 RLLDLKNNRIKQlegiLRSH-DLPTSE--QLKDVAYGTRPLSLCLETLPAH-GDEDKVDISLLHQGENLFEL 630
Cdd:pfam15921  510 RAIEATNAEITK----LRSRvDLKLQElqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL 577
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
328-579 7.21e-03

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


Pssm-ID: 308206  Cd Length: 1162  Bit Score: 40.73  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   328 ELRAELKEESKKAVSLKSQLEDVSILQMTLKefqERVEDLEKERKLLNDNYDKL------LESMLDSSDSSSQPHWSNEL 401
Cdd:pfam02463  167 RLKRKKKEALKKLIEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKekleleEEYLLYLDYLKLNEERIDLL 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   402 IAEQLQQQVSQLQDQLDAELE-----DKRKVLLELSREKAQNEDLKLEVTNILQKHKQEVELLQNAATISQppDRQSEPA 476
Cdd:pfam02463  244 QELLRDEQEEIESSKQEIEKEeeklaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE--EKLKESE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112734867   477 THPAVLQENTQIEPSEPKNQEEKKLSQVLNELQVSHAETTLELEKTRDMLILQRKI---------NVCYQEELEAMMTKA 547
Cdd:pfam02463  322 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakkkleserLSSAAKLKEEELELK 401
                          250       260       270
                   ....*....|....*....|....*....|..
gi 112734867   548 DNDNRDHKEKLERLTRLLDLKNNRIKQLEGIL 579
Cdd:pfam02463  402 SEEEKEAQLLLELARQLEDLLKEEKKEELEIL 433
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
321-385 9.09e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 308162  Cd Length: 107  Bit Score: 37.18  E-value: 9.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112734867   321 ALLKQVNELRAELKEESKKAVSLKSQLEDVSILQMTLKEFQERVEDLEKERKLLNDNYDKLLESM 385
Cdd:pfam02403   39 ELQVELEELQAERNELSKEIGQAKKKKEDAEALIAEVKELKDELKALEAELKELEAELDKLLLAI 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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